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

Protein record

ZMYND11

Zinc finger MYND domain-containing protein 11

Q15326 at UniProt
Homo sapiens602 amino acidsannotation supported
1annotated core in ZMYND11
1PDB entries with observed PWWP1 coordinates
6model records for PWWP1
0frozen v1.2 assay / association records for PWWP1

Canonical sequence · Source-mapped regions

Protein domain architecture

602 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 · 280–331 · UniProtKB reviewed feature · annotation core; not a certified complete folded domain or pocket Other source annotations Domain: SAMD1-like winged helix (WH) · 6–82 · UniProtKB source annotation Zinc finger: PHD-type · 100–148 · UniProtKB source annotation Domain: Bromo · 149–255 · UniProtKB source annotation Zinc finger: MYND-type · 563–598 · UniProtKB source annotation 1 150 301 452 602
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
SAMD1-like winged helix (WH)Domain6–82ECO:0000255 PROSITE-ProRule: PRU01358
PHD-typeZinc finger100–148ECO:0000255 PROSITE-ProRule: PRU00146
BromoDomain149–255ECO:0000255 PROSITE-ProRule: PRU00035
MYND-typeZinc finger563–598ECO:0000255 PROSITE-ProRule: PRU00134
ECO:0000269 PubMed: 26845565

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.

4NS5chain A154–371
Mapped deposited segment 154–371 Observed canonical residues 156–171Observed canonical residues 196–364
Mapping and construct evidence

Deposited polymer length: 227 residues. Mapped sequence identity: 100.0%. sequence differences or tags detected; biological versus engineered origin requires review.

PWWP1: 52 / 52 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, 220–227.

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

Validated isoform differences · 5 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
Q15326-2548PWWP1226–277
52 / 52 mapped residues; span may contain gaps		complete
Q15326-3568PWWP1280–331
52 / 52 mapped residues; span may contain gaps		complete
Q15326-4514PWWP1226–277
52 / 52 mapped residues; span may contain gaps		complete
Q15326-5517PWWP1195–246
52 / 52 mapped residues; span may contain gaps		complete
Q15326-6567PWWP1279–330
52 / 52 mapped residues; span may contain gaps		complete
Viewing ZMYND11 PWWP1

Canonical annotation interval 280–331 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.

Alternative PWWP annotations and interval provenance
[
  {
    "end": 359,
    "identifier": "IPR047268",
    "integrated_identifier": null,
    "model": null,
    "name": "Zinc finger MYND domain-containing protein 11, PWWP domain",
    "representative": false,
    "score": null,
    "source": "interpro",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q15326/?page_size=200",
    "start": 275
  },
  {
    "end": 359,
    "identifier": "cd20159",
    "integrated_identifier": "IPR047268",
    "model": "cd20159",
    "name": "PWWP domain found in protein BS69 and similar proteins",
    "representative": false,
    "score": 8.6586e-54,
    "source": "cdd",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q15326/?page_size=200",
    "start": 275
  },
  {
    "end": 329,
    "identifier": "SM00293",
    "integrated_identifier": "IPR000313",
    "model": "SM00293",
    "name": "domain with conserved PWWP motif",
    "representative": false,
    "score": 3.5e-21,
    "source": "smart",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q15326/?page_size=200",
    "start": 278
  },
  {
    "end": 350,
    "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/Q15326/?page_size=200",
    "start": 278
  },
  {
    "end": 331,
    "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/Q15326/?page_size=200",
    "start": 280
  },
  {
    "end": 350,
    "identifier": "PF00855",
    "integrated_identifier": "IPR000313",
    "model": "PF00855",
    "name": "PWWP domain",
    "representative": false,
    "score": 2.8e-07,
    "source": "pfam",
    "source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/Q15326/?page_size=200",
    "start": 282
  }
]

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.

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
4NS5A52 / 52APOX-RAY DIFFRACTION
1.9 Å		0.245No 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

6 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-Q15326-F1:v6
Canonical		GDMcomplete96.582.3
AF-Q15326-2-F1:v6GDMcomplete95.679
AF-Q15326-3-F1:v6GDMcomplete96.881.7
AF-Q15326-4-F1:v6GDMcomplete96.578.5
AF-Q15326-5-F1:v6GDMcomplete96.278
AF-Q15326-6-F1:v6GDMcomplete96.881.1

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 ZMYND11 PWWP1512.390.444 / 0.705Aligned core viewer
BRD1 PWWP1 ZMYND11 PWWP1481.870.501 / 0.756Aligned core viewer
BRPF1 PWWP1 ZMYND11 PWWP1501.980.515 / 0.774Aligned core viewer
BRPF3 PWWP1 ZMYND11 PWWP1512.20.523 / 0.794Aligned core viewer
DNMT3A PWWP1 ZMYND11 PWWP1511.810.725 / 0.807Aligned core viewer
DNMT3B PWWP1 ZMYND11 PWWP1511.890.705 / 0.781Aligned core viewer
HDGF PWWP1 ZMYND11 PWWP1512.420.631 / 0.682Aligned core viewer
HDGFL2 PWWP1 ZMYND11 PWWP1512.080.687 / 0.747Aligned core viewer
HDGFL3 PWWP1 ZMYND11 PWWP1512.120.689 / 0.749Aligned core viewer
MSH6 PWWP1 ZMYND11 PWWP1522.270.663 / 0.773Aligned core viewer
NSD2 PWWP1 ZMYND11 PWWP1511.720.673 / 0.812Aligned core viewer
NSD3 PWWP1 ZMYND11 PWWP1521.850.697 / 0.833Aligned core viewer
NSD3 PWWP2 ZMYND11 PWWP1502.810.596 / 0.694Aligned core viewer
PSIP1 PWWP1 ZMYND11 PWWP1502.090.634 / 0.747Aligned core viewer
PWWP2B PWWP1 ZMYND11 PWWP1511.580.713 / 0.815Aligned core viewer
PWWP3A PWWP1 ZMYND11 PWWP1512.10.64 / 0.731Aligned core viewer
ZMYND11 PWWP1 ZMYND8 PWWP1511.390.848 / 0.862Aligned core viewer