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

Protein record

BRPF1

Peregrin

P55201 at UniProt
Homo sapiens1214 amino acidsannotation supported
1annotated core in BRPF1
7PDB entries with observed PWWP1 coordinates
4model records for PWWP1
0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

1214 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 · 1085–1168 · UniProtKB reviewed feature · annotation core; not a certified complete folded domain or pocket Other source annotations Zinc finger: C2H2-type · 21–47 · UniProtKB source annotation Zinc finger: PHD-type 1 · 273–323 · UniProtKB source annotation Zinc finger: C2HC pre-PHD-type · 327–360 · UniProtKB source annotation Zinc finger: PHD-type 2 · 384–448 · UniProtKB source annotation Domain: Bromo · 628–732 · UniProtKB source annotation 1 304 607 910 1214
PWWP annotation coreOther source annotationPredicted candidate, when present
5 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.

Source featureTypeAmino acidsEvidence
C2H2-typeZinc finger21–47ECO:0000255 PROSITE-ProRule: PRU00042
PHD-type 1Zinc finger273–323ECO:0000255 PROSITE-ProRule: PRU00146
C2HC pre-PHD-typeZinc finger327–360ECO:0000255 PROSITE-ProRule: PRU01146
PHD-type 2Zinc finger384–448ECO:0000255 PROSITE-ProRule: PRU01146
BromoDomain628–732ECO:0000255 PROSITE-ProRule: PRU00035

Deposited construct mapping

2 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.

3L42chain A1079–1207
Mapped deposited segment 1079–1207 Observed canonical residues 1079–1205
Mapping and construct evidence

Deposited polymer length: 130 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 84 / 84 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.

2X35chain A1076–1205
Mapped deposited segment 1076–1205 Observed canonical residues 1080–1204
Mapping and construct evidence

Deposited polymer length: 132 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 84 / 84 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: 1–2.

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

Validated isoform differences · 3 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
P55201-21220PWWP11091–1174
84 / 84 mapped residues; span may contain gaps		complete
P55201-31213PWWP11084–1167
84 / 84 mapped residues; span may contain gaps		complete
P55201-41119PWWP1990–1073
84 / 84 mapped residues; span may contain gaps		complete
Viewing BRPF1 PWWP1

Canonical annotation interval 1085–1168 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 1166,
    "identifier": "SM00293",
    "integrated_identifier": "IPR000313",
    "model": "SM00293",
    "name": "domain with conserved PWWP motif",
    "representative": false,
    "score": 7.2e-42,
    "source": "smart",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P55201/?page_size=200",
    "start": 1083
  },
  {
    "end": 1196,
    "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/P55201/?page_size=200",
    "start": 1083
  },
  {
    "end": 1202,
    "identifier": "IPR049583",
    "integrated_identifier": null,
    "model": null,
    "name": "Peregrin, PWWP domain",
    "representative": false,
    "score": null,
    "source": "interpro",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P55201/?page_size=200",
    "start": 1083
  },
  {
    "end": 1202,
    "identifier": "cd20156",
    "integrated_identifier": "IPR049583",
    "model": "cd20156",
    "name": "PWWP domain found in bromodomain and PHD finger-containing protein 1 (BRPF1)",
    "representative": false,
    "score": 7.17526e-83,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P55201/?page_size=200",
    "start": 1083
  },
  {
    "end": 1168,
    "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/P55201/?page_size=200",
    "start": 1085
  },
  {
    "end": 1196,
    "identifier": "PF00855",
    "integrated_identifier": "IPR000313",
    "model": "PF00855",
    "name": "PWWP domain",
    "representative": false,
    "score": 2e-11,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/P55201/?page_size=200",
    "start": 1087
  }
]

PWWP1 · source-classified Phase 6A evidence

Ligands & Bioactivity

Explore all domain compounds →

2 chemical or preparation profiles · 1 domain-attributed assay / association observations. Counts refer to the curated snapshot.

0 profiles

Experiment-specific controls

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

0 profiles

Ambiguous / indirect evidence

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.

FORMIC ACID · Other PDB component · not a studied ligand4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID · Other PDB component · not a studied ligandSULFATE ION · Other PDB component · not a studied ligandCHLORIDE ION · Other PDB component · not a studied ligand

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

7 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
2X35A84 / 84APOX-RAY DIFFRACTION
2.0 Å		0.642No classification flag
2X4WA84 / 84ComplexesX-RAY DIFFRACTION
1.5 Å		0.482No classification flag
2X4XA84 / 84ComplexesX-RAY DIFFRACTION
1.85 Å		0.414No classification flag
2X4YA84 / 84ComplexesX-RAY DIFFRACTION
1.7 Å		0.442No classification flag
3L42A84 / 84Unclassified_ReviewX-RAY DIFFRACTION
1.3 Å		0.64Required
3MO8A84 / 84ComplexesX-RAY DIFFRACTION
1.69 Å		0.543No classification flag
5C6SA84 / 84Co-CrystalsX-RAY DIFFRACTION
1.3 Å		0.556Required

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
No curated assay row for this domain. This does not establish that no literature evidence exists.

Scientific review queue

PWWP1 · Prediction evidence

Predicted models

4 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-P55201-F1:v6
Canonical		GDMcomplete89.967.5
AF-P55201-2-F1:v6GDMcomplete89.267.1
AF-P55201-3-F1:v6GDMcomplete89.967.3
AF-P55201-4-F1:v6GDMcomplete90.370.5

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 BRPF1 PWWP1591.940.521 / 0.567Aligned core viewer
BRD1 PWWP1 BRPF1 PWWP1781.620.851 / 0.851Aligned core viewer
BRPF1 PWWP1 BRPF3 PWWP1840.780.958 / 0.958Aligned core viewer
BRPF1 PWWP1 DNMT3A PWWP1581.80.598 / 0.811Aligned core viewer
BRPF1 PWWP1 DNMT3B PWWP1591.90.596 / 0.807Aligned core viewer
BRPF1 PWWP1 HDGF PWWP1572.540.526 / 0.702Aligned core viewer
BRPF1 PWWP1 HDGFL2 PWWP1581.840.59 / 0.812Aligned core viewer
BRPF1 PWWP1 HDGFL3 PWWP1582.180.578 / 0.794Aligned core viewer
BRPF1 PWWP1 MSH6 PWWP1612.630.575 / 0.735Aligned core viewer
BRPF1 PWWP1 NSD2 PWWP1592.150.587 / 0.733Aligned core viewer
BRPF1 PWWP1 NSD3 PWWP1592.120.595 / 0.752Aligned core viewer
BRPF1 PWWP1 NSD3 PWWP2632.10.631 / 0.805Aligned core viewer
BRPF1 PWWP1 PSIP1 PWWP1561.940.558 / 0.701Aligned core viewer
BRPF1 PWWP1 PWWP2B PWWP1542.170.544 / 0.721Aligned core viewer
BRPF1 PWWP1 PWWP3A PWWP1512.290.483 / 0.616Aligned core viewer
BRPF1 PWWP1 ZMYND11 PWWP1501.980.515 / 0.774Aligned core viewer
BRPF1 PWWP1 ZMYND8 PWWP1512.250.507 / 0.773Aligned core viewer