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

Protein record

BRD1

Bromodomain-containing protein 1

O95696 at UniProt
Homo sapiens1058 amino acidsannotation supported
1annotated core in BRD1
3PDB entries with observed PWWP1 coordinates
2model records for PWWP1
0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

1058 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 · 929–1012 · UniProtKB reviewed feature · annotation core; not a certified complete folded domain or pocket Other source annotations Zinc finger: PHD-type 1 · 214–264 · UniProtKB source annotation Zinc finger: C2HC pre-PHD-type · 268–301 · UniProtKB source annotation Zinc finger: PHD-type 2 · 325–389 · UniProtKB source annotation Domain: Bromo · 562–666 · UniProtKB source annotation 1 264 529 794 1058
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 finger214–264ECO:0000255 PROSITE-ProRule: PRU00146
C2HC pre-PHD-typeZinc finger268–301ECO:0000255 PROSITE-ProRule: PRU01146
PHD-type 2Zinc finger325–389ECO:0000255 PROSITE-ProRule: PRU01146
BromoDomain562–666ECO: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.

4Z02chain A925–1049
Mapped deposited segment 925–1049 Observed canonical residues 929–1047
Mapping and construct evidence

Deposited polymer length: 125 residues. Mapped sequence identity: 100.0%. no sequence difference detected by mapping; not proof of wild type.

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.

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

Validated isoform differences · 1 PWWP correspondence record

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
O95696-21189PWWP11060–1143
84 / 84 mapped residues; span may contain gaps		complete
Viewing BRD1 PWWP1

Canonical annotation interval 929–1012 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 1010,
    "identifier": "SM00293",
    "integrated_identifier": "IPR000313",
    "model": "SM00293",
    "name": "domain with conserved PWWP motif",
    "representative": false,
    "score": 9.7e-40,
    "source": "smart",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O95696/?page_size=200",
    "start": 927
  },
  {
    "end": 1037,
    "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/O95696/?page_size=200",
    "start": 927
  },
  {
    "end": 1046,
    "identifier": "cd20157",
    "integrated_identifier": null,
    "model": "cd20157",
    "name": "PWWP domain found in bromodomain and PHD finger-containing protein 2 (BRPF2)",
    "representative": false,
    "score": 1.44198e-84,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O95696/?page_size=200",
    "start": 927
  },
  {
    "end": 1012,
    "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/O95696/?page_size=200",
    "start": 929
  },
  {
    "end": 1037,
    "identifier": "PF00855",
    "integrated_identifier": "IPR000313",
    "model": "PF00855",
    "name": "PWWP domain",
    "representative": false,
    "score": 4.5e-10,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/O95696/?page_size=200",
    "start": 931
  }
]

PWWP1 · source-classified Phase 6A evidence

Ligands & Bioactivity

Explore all domain compounds →

1 chemical or preparation profiles · 0 domain-attributed assay / association observations. Counts refer to 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.

1,2-ETHANEDIOL · Other PDB component · not a studied ligand

Open this domain in Structural & Binding Landscape →

PWWP1 · Deposited coordinates

Experimental coverage and AlphaFold correspondence

3 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
3LYIA84 / 84Unclassified_ReviewX-RAY DIFFRACTION
2.1 Å		3.3Required
4Z02A84 / 84Co-CrystalsX-RAY DIFFRACTION
1.87 Å		3.35Required
7LH9B84 / 84ComplexesX-RAY DIFFRACTION
2.6 Å		1.09No 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

2 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-O95696-F1:v6
Canonical		GDMcomplete86.571.5
AF-O95696-2-F1:v6GDMcomplete84.267.7

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 BRD1 PWWP1592.160.501 / 0.543Aligned core viewer
BRD1 PWWP1 BRPF1 PWWP1781.620.851 / 0.851Aligned core viewer
BRD1 PWWP1 BRPF3 PWWP1822.360.835 / 0.835Aligned core viewer
BRD1 PWWP1 DNMT3A PWWP1592.550.568 / 0.768Aligned core viewer
BRD1 PWWP1 DNMT3B PWWP1592.520.569 / 0.766Aligned core viewer
BRD1 PWWP1 HDGF PWWP1563.00.504 / 0.677Aligned core viewer
BRD1 PWWP1 HDGFL2 PWWP1582.480.56 / 0.766Aligned core viewer
BRD1 PWWP1 HDGFL3 PWWP1582.880.549 / 0.754Aligned core viewer
BRD1 PWWP1 MSH6 PWWP1592.730.556 / 0.712Aligned core viewer
BRD1 PWWP1 NSD2 PWWP1582.450.56 / 0.697Aligned core viewer
BRD1 PWWP1 NSD3 PWWP1572.210.563 / 0.707Aligned core viewer
BRD1 PWWP1 NSD3 PWWP2632.450.6 / 0.76Aligned core viewer
BRD1 PWWP1 PSIP1 PWWP1572.660.537 / 0.673Aligned core viewer
BRD1 PWWP1 PWWP2B PWWP1542.890.514 / 0.677Aligned core viewer
BRD1 PWWP1 PWWP3A PWWP1512.910.464 / 0.592Aligned core viewer
BRD1 PWWP1 ZMYND11 PWWP1481.870.501 / 0.756Aligned core viewer
BRD1 PWWP1 ZMYND8 PWWP1492.220.49 / 0.747Aligned core viewer