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

Native domain record

BRPF3 PWWP1

Bromodomain and PHD finger-containing protein 3

Q9ULD4 at UniProt
Homo sapiens1205 amino acidsannotation supportedUP:Q9ULD4:PWWP1
1annotated core in BRPF3
1PDB entries with observed PWWP1 coordinates
3model records for PWWP1
0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

1205 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 · 1076–1159 · UniProtKB reviewed feature · annotation core; not a certified complete folded domain or pocket Other source annotations Zinc finger: PHD-type 1 · 212–262 · UniProtKB source annotation Zinc finger: C2HC pre-PHD-type · 266–299 · UniProtKB source annotation Zinc finger: PHD-type 2 · 323–387 · UniProtKB source annotation Domain: Bromo · 589–693 · UniProtKB source annotation 1 301 602 904 1205
PWWP annotation coreOther source annotationPredicted candidate, when present
4 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
PHD-type 1Zinc finger212–262ECO:0000255 PROSITE-ProRule: PRU00146
C2HC pre-PHD-typeZinc finger266–299ECO:0000255 PROSITE-ProRule: PRU01146
PHD-type 2Zinc finger323–387ECO:0000255 PROSITE-ProRule: PRU01146
BromoDomain589–693ECO:0000255 PROSITE-ProRule: PRU00035

Deposited construct mapping

1 selected example

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.

3PFSchain A1056–1195
Mapped deposited segment 1056–1195 Observed canonical residues 1061–1194
Mapping and construct evidence

Deposited polymer length: 158 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: 1–18.

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
Q9ULD4-2935PWWP1806–889
84 / 84 mapped residues; span may contain gaps		complete
Q9ULD4-3871PWWP1742–825
84 / 84 mapped residues; span may contain gaps		complete
Viewing BRPF3 PWWP1

Canonical annotation interval 1076–1159 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 1157,
    "identifier": "SM00293",
    "integrated_identifier": "IPR000313",
    "model": "SM00293",
    "name": "domain with conserved PWWP motif",
    "representative": false,
    "score": 1.2e-38,
    "source": "smart",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q9ULD4/?page_size=200",
    "start": 1074
  },
  {
    "end": 1186,
    "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/Q9ULD4/?page_size=200",
    "start": 1074
  },
  {
    "end": 1191,
    "identifier": "cd20158",
    "integrated_identifier": null,
    "model": "cd20158",
    "name": "PWWP domain found in bromodomain and PHD finger-containing protein 3 (BRPF3)",
    "representative": false,
    "score": 1.46312e-83,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q9ULD4/?page_size=200",
    "start": 1074
  },
  {
    "end": 1159,
    "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/Q9ULD4/?page_size=200",
    "start": 1076
  },
  {
    "end": 1186,
    "identifier": "PF00855",
    "integrated_identifier": "IPR000313",
    "model": "PF00855",
    "name": "PWWP domain",
    "representative": false,
    "score": 5.3e-11,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q9ULD4/?page_size=200",
    "start": 1078
  }
]

PWWP1 · source-classified Phase 6A evidence

Ligands & Bioactivity

Explore all domain compounds →

0 chemical or preparation profiles · 0 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

Studied without research structure

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.

0 profiles

Ambiguous / indirect evidence

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

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

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

SULFATE ION · Other PDB component · not a studied ligand

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

1 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
3PFSA84 / 84APOX-RAY DIFFRACTION
1.9 Å		0.595No classification flag

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

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-Q9ULD4-F1:v6
Canonical		GDMcomplete9067.1
AF-Q9ULD4-2-F1:v6GDMcomplete90.272.1
AF-Q9ULD4-3-F1:v6GDMcomplete90.274.7

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 BRPF3 PWWP1591.830.526 / 0.572Aligned core viewer
BRD1 PWWP1 BRPF3 PWWP1822.360.835 / 0.835Aligned core viewer
BRPF1 PWWP1 BRPF3 PWWP1840.780.958 / 0.958Aligned core viewer
BRPF3 PWWP1 DNMT3A PWWP1581.770.599 / 0.814Aligned core viewer
BRPF3 PWWP1 DNMT3B PWWP1591.870.595 / 0.803Aligned core viewer
BRPF3 PWWP1 HDGF PWWP1572.60.526 / 0.702Aligned core viewer
BRPF3 PWWP1 HDGFL2 PWWP1581.770.585 / 0.799Aligned core viewer
BRPF3 PWWP1 HDGFL3 PWWP1582.190.57 / 0.781Aligned core viewer
BRPF3 PWWP1 MSH6 PWWP1622.560.574 / 0.727Aligned core viewer
BRPF3 PWWP1 NSD2 PWWP1622.640.582 / 0.719Aligned core viewer
BRPF3 PWWP1 NSD3 PWWP1592.060.593 / 0.746Aligned core viewer
BRPF3 PWWP1 NSD3 PWWP2631.950.638 / 0.817Aligned core viewer
BRPF3 PWWP1 PSIP1 PWWP1561.970.564 / 0.712Aligned core viewer
BRPF3 PWWP1 PWWP2B PWWP1531.980.535 / 0.704Aligned core viewer
BRPF3 PWWP1 PWWP3A PWWP1512.220.479 / 0.609Aligned core viewer
BRPF3 PWWP1 ZMYND11 PWWP1512.20.523 / 0.794Aligned core viewer
BRPF3 PWWP1 ZMYND8 PWWP1512.190.512 / 0.786Aligned core viewer