PWWPAtlas
STRUCTURAL BIOLOGY & CHEMICAL EVIDENCEDataset v1.2 · Phase 6D · Comparative experimental recognition environments

Protein record

PSIP1

PC4 and SFRS1-interacting protein

O75475 at UniProt
Homo sapiens530 amino acidsannotation supported
1annotated core in PSIP1
13PDB entries with observed PWWP1 coordinates
3model records for PWWP1
3frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

530 residues

PWWP annotation cores, other annotated regions, and deposited construct mappings share the canonical amino acid axis. The original Atlas PWWP intervals retain their source definitions.

PWWP annotation cores PWWP1 · 1–64 · UniProtKB reviewed feature · annotation core; not a certified complete folded domain or pocket Other source annotations No additional eligible domain features in the retrieved source. 1 132 265 398 530
PWWP annotation coreOther source annotationPredicted candidate, when present
0 additional source-supported regions · coordinates and evidence

UniProt feature coordinates accepted after exact canonical sequence identity check against the frozen Atlas. Source annotations can be inferred by sequence or curated from experiments; evidence codes remain attached. Other domain types link to their UniProt source because the Atlas records PWWP domains.

Deposited construct mapping

4 selected examples

Colored segments map deposited polymer sequences to this canonical protein; dark segments have observed coordinates. Unmapped tags and engineered residues are not assigned canonical positions. These are not certified whole-fold boundaries.

2M16chain A1–93
Mapped deposited segment 1–93 Observed canonical residues 1–93
Mapping and construct evidence

Deposited polymer length: 97 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 64 / 64 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–4.

9S83chain B1–90
Mapped deposited segment 1–90 Observed canonical residues 2–90
Mapping and construct evidence

Deposited polymer length: 91 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 63 / 64 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–1.

3ZEHchain A3–100
Mapped deposited segment 3–100 Observed canonical residues 3–93
Mapping and construct evidence

Deposited polymer length: 105 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 62 / 64 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–7.

4FU6chain A1–135
Mapped deposited segment 1–135 Observed canonical residues 1–30Observed canonical residues 33–91
Mapping and construct evidence

Deposited polymer length: 153 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 62 / 64 annotation-core Cα residues observed.

Frozen SIFTS aligned regions with construct-to-UniProt sequence comparison. Bars are mapped canonical segments; tags, insertions, and unmapped termini are not assigned canonical positions. PDB source.

Unmapped construct positions: 1–18.

One mapped example per native domain, preferring frozen experimental representatives; up to four distinct mapped intervals.

Validated isoform differences · 2 PWWP correspondence records

Only source-validated PWWP core correspondences from the frozen v1.2 isoform audit; other-domain architectures are not projected onto isoforms. Coordinates in the isoform column refer to the individual isoform sequence; deleted cores remain absent.

IsoformLengthPWWP coreSource-mapped positionsRetention / source edits
O75475-2333PWWP11–64
64 / 64 mapped residues; span may contain gaps		complete
O75475-3329PWWP11–64
64 / 64 mapped residues; span may contain gaps		complete
Viewing PSIP1 PWWP1

Canonical annotation interval 1–64 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 62,
    "identifier": "SM00293",
    "integrated_identifier": "IPR000313",
    "model": "SM00293",
    "name": "domain with conserved PWWP motif",
    "representative": false,
    "score": 3.5e-17,
    "source": "smart",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O75475/?page_size=200",
    "start": 5
  },
  {
    "end": 87,
    "identifier": "IPR000313",
    "integrated_identifier": null,
    "model": null,
    "name": "PWWP domain",
    "representative": false,
    "score": null,
    "source": "interpro",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O75475/?page_size=200",
    "start": 5
  },
  {
    "end": 92,
    "identifier": "cd20151",
    "integrated_identifier": null,
    "model": "cd20151",
    "name": "PWWP domain found in PC4 and SFRS1-interacting protein (PSIP)",
    "representative": false,
    "score": 5.28658e-64,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O75475/?page_size=200",
    "start": 5
  },
  {
    "end": 64,
    "identifier": "PS50812",
    "integrated_identifier": "IPR000313",
    "model": "PS50812",
    "name": "PWWP domain profile",
    "representative": false,
    "score": null,
    "source": "profile",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O75475/?page_size=200",
    "start": 7
  },
  {
    "end": 87,
    "identifier": "PF00855",
    "integrated_identifier": "IPR000313",
    "model": "PF00855",
    "name": "PWWP domain",
    "representative": false,
    "score": 1.8e-12,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O75475/?page_size=200",
    "start": 8
  }
]

PWWP1 · source-classified Phase 6A evidence

Ligands & Bioactivity

Explore all domain compounds →

2 chemical or preparation profiles · 2 domain-attributed assay / association observations. Counts refer to the curated snapshot.

0 profiles

Deposited research ligands

No records in this category for the selected domain in the curated snapshot.

0 profiles

Experiment-specific controls

No records in this category for the selected domain in the curated snapshot.

4 other deposited components in this domain (not pharmacological ligands)

Buffers, ions, cryoprotectants and solvents remain recorded as deposited chemical components.

1,2-ETHANEDIOL · Other PDB component · not a studied ligandGLYCEROL · Other PDB component · not a studied ligand3-CYCLOHEXYL-1-PROPYLSULFONIC ACID · Other PDB component · not a studied ligandSULFATE ION · Other PDB component · not a studied ligand
1 protein-level observations — no specific PWWP-domain attribution

These observations concern PSIP1 in its reported experimental context. They are excluded from the selected domain's measurement counts.

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

19 entry / domain records

One representative chain per PDB entry and native domain. RMSD uses fixed UniProt correspondence and all common Cα atoms; it is reported only for ≥40 atoms and ≥80% core coverage. A value is descriptive, not a prediction benchmark.

PDBChainObserved core CαClassMethod / resolutionAF RMSD ÅReview
2M16A64 / 64APOSOLUTION NMR1.77No classification flag
9S83B63 / 64ComplexesX-RAY DIFFRACTION
2.1 Å		1.37No classification flag
3ZEHA62 / 64APOSOLUTION NMR1.58No classification flag
4FU6A62 / 64Unclassified_ReviewX-RAY DIFFRACTION
2.1 Å		1.62Required
9S81A61 / 64APOX-RAY DIFFRACTION
1.63 Å		0.95No classification flag
6S01K59 / 64ComplexesELECTRON MICROSCOPY
3.2 Å		2.55No classification flag
8CBNI59 / 64ComplexesELECTRON MICROSCOPY
3.34 Å		2.55No classification flag
8CBQI59 / 64ComplexesELECTRON MICROSCOPY
4.0 Å		2.55No classification flag
8PC5J59 / 64ComplexesELECTRON MICROSCOPY
3.02 Å		2.23No classification flag
8PC6J59 / 64ComplexesELECTRON MICROSCOPY
3.04 Å		2.25No classification flag
8PEOJ59 / 64ComplexesELECTRON MICROSCOPY
2.69 Å		2.18No classification flag
8PEPJ59 / 64ComplexesELECTRON MICROSCOPY
3.33 Å		2.25No classification flag
9XYCK58 / 64ComplexesELECTRON MICROSCOPY
3.5 Å		2.26No classification flag
7OUFC0 / 64Unclassified_ReviewELECTRON MICROSCOPY
3.0 Å		—Required
7OUGC0 / 64Unclassified_ReviewELECTRON MICROSCOPY
3.1 Å		—Required
7OUHC0 / 64Unclassified_ReviewELECTRON MICROSCOPY
3.5 Å		—Required
7PELC0 / 64Unclassified_ReviewELECTRON MICROSCOPY
3.34 Å		—Required
9S28Q0 / 64Unclassified_ReviewELECTRON MICROSCOPY
2.8 Å		—Required
9S29AA0 / 64Unclassified_ReviewELECTRON MICROSCOPY
2.8 Å		—Required

PWWP1 · Measured preparations

Frozen v1.2 assay records

Explore evidence links

This retained table is the original source projection. The Phase 5 Ligands & Bioactivity section above includes added observations and reviewed target context. Values remain attached to their assay, construct and preparation. A crystal structure does not transfer affinity to another construct or stereoisomer. Assay pages preserve field-level source-verification states where reviewed; unreviewed null fields remain uncurated.

Preparation / identityAssay and resultConstructEvidence and source
BPP
exact single CCD identity		ITC Kd
= 27.0 µM ± 2.0
direct binding affinity		UncuratedPMID:39031937
primary_publisher_selected_indexed_Results_and_Methods_passages; Figure S2 not independently retrieved

Full assay buffer, temperature and incubation metadata not transcribed; null means uncurated, not absent.

Assay conditions and interpretation

{}

Binding is established in solution; no PSIP1–BPP crystal structure is assigned here.

NbH10
named macromolecule no full sequence identity		SPR apparent Kd
= 94.4 nM ± 9.1
direct binding affinity		1–90PMID:42194065
local_primary_full_text_XML_table_and_methods_verified
Assay conditions and interpretation

{"protein_construct": "PSIP1 1–90", "replicates": 3, "uncertainty_type": "SD"}

Apparent SPR affinity of a nanobody; not a small molecule or a solved nanobody–PWWP complex.

NbH10
named macromolecule no full sequence identity		AlphaScreen inhibition IC50
= 0.94 µM ± 0.15
biochemical interaction inhibition		UncuratedPMID:42194065
local_primary_full_text_XML; Table 1, methods and Results inspected

Full assay buffer, temperature and incubation metadata not transcribed; null means uncurated, not absent.

Assay conditions and interpretation

{"partner": "H3K36me3 nucleosomes", "protein": "full-length LEDGF/p75"}

Macromolecular binder. NbH10-alone crystal coordinates do not establish a PWWP-bound complex.

Scientific review queue

PWWP1 · Prediction evidence

Predicted models

3 model records

Domain retention uses independently reconstructed UniProt isoform edits. Local pLDDT is not experimental confirmation and does not establish interdomain orientation.

ModelOriginCore retentionCore mean pLDDTFull mean pLDDTCautions
AF-O75475-F1:v6
Canonical		GDMcomplete88.562.6
AF-O75475-2-F1:v6GDMcomplete8964
AF-O75475-3-F1:v6GDMcomplete89.162.6

PWWP1 · Structural correspondence

Human annotation-core comparisons

17 pairs

Structural alignment establishes a residue correspondence for these cropped cores. It does not establish equivalent ligand pockets, function or selectivity.

Domain pairAligned CαUS-align RMSD ÅTM score A / BView
ARID4A PWWP1 PSIP1 PWWP1602.420.504 / 0.67Aligned core viewer
BRD1 PWWP1 PSIP1 PWWP1572.660.537 / 0.673Aligned core viewer
BRPF1 PWWP1 PSIP1 PWWP1561.940.558 / 0.701Aligned core viewer
BRPF3 PWWP1 PSIP1 PWWP1561.970.564 / 0.712Aligned core viewer
DNMT3A PWWP1 PSIP1 PWWP1561.70.775 / 0.726Aligned core viewer
DNMT3B PWWP1 PSIP1 PWWP1571.980.775 / 0.726Aligned core viewer
HDGF PWWP1 PSIP1 PWWP1571.80.743 / 0.69Aligned core viewer
HDGFL2 PWWP1 PSIP1 PWWP1571.750.801 / 0.739Aligned core viewer
HDGFL3 PWWP1 PSIP1 PWWP1571.530.788 / 0.73Aligned core viewer
MSH6 PWWP1 PSIP1 PWWP1562.50.659 / 0.652Aligned core viewer
NSD2 PWWP1 PSIP1 PWWP1542.230.646 / 0.654Aligned core viewer
NSD3 PWWP1 PSIP1 PWWP1562.530.654 / 0.654Aligned core viewer
NSD3 PWWP2 PSIP1 PWWP1572.650.666 / 0.658Aligned core viewer
PSIP1 PWWP1 PWWP2B PWWP1501.860.637 / 0.662Aligned core viewer
PSIP1 PWWP1 PWWP3A PWWP1502.370.593 / 0.607Aligned core viewer
PSIP1 PWWP1 ZMYND11 PWWP1502.090.634 / 0.747Aligned core viewer
PSIP1 PWWP1 ZMYND8 PWWP1511.980.636 / 0.758Aligned core viewer