0 profiles
Deposited research ligands
No records in this category for the selected domain in the curated snapshot.
Native domain record
Putative PWWP domain-containing DNA repair factor 4
Canonical sequence · Source-mapped regions
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.
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.
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.
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.
No source-validated alternative-isoform core mapping is available in this snapshot.
Canonical annotation interval 1756–1817 · UniProtKB reviewed feature. annotation core; not a certified complete folded domain or pocket.
[
{
"end": 1841,
"identifier": "IPR035504",
"integrated_identifier": null,
"model": null,
"name": "MUM1-like, PWWP domain",
"representative": false,
"score": null,
"source": "interpro",
"source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/A0A494C071/?page_size=200",
"start": 1754
},
{
"end": 1841,
"identifier": "cd06080",
"integrated_identifier": "IPR035504",
"model": "cd06080",
"name": "PWWP domain found in mutated melanoma-associated antigen 1 (MUM-1) and similar proteins",
"representative": false,
"score": 3.21906e-27,
"source": "cdd",
"source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/A0A494C071/?page_size=200",
"start": 1754
},
{
"end": 1833,
"identifier": "PF20884",
"integrated_identifier": "IPR035504",
"model": "PF20884",
"name": "MUM1-like, PWWP domain",
"representative": false,
"score": 1.9e-24,
"source": "pfam",
"source_url": "https://www.ebi.ac.uk/interpro/api/entry/all/protein/uniprot/A0A494C071/?page_size=200",
"start": 1755
}
]PWWP1 · source-classified Phase 6A evidence
0 chemical or preparation profiles · 0 domain-attributed assay / association observations. Counts refer to the curated snapshot.
0 profiles
No records in this category for the selected domain in the curated snapshot.
0 profiles
No records in this category for the selected domain in the curated snapshot.
0 profiles
No records in this category for the selected domain in the curated snapshot.
0 profiles
No records in this category for the selected domain in the curated snapshot.
PWWP1 · Deposited coordinates
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.
| PDB | Chain | Observed core Cα | Class | Method / resolution | AF RMSD Å | Review |
|---|---|---|---|---|---|---|
| No experimental entry is mapped to this domain in the frozen snapshot. | ||||||
PWWP1 · Measured preparations
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 / identity | Assay and result | Construct | Evidence and source |
|---|---|---|---|
| No curated assay row for this domain. This does not establish that no literature evidence exists. | |||
PWWP1 · Prediction evidence
Domain retention uses independently reconstructed UniProt isoform edits. Local pLDDT is not experimental confirmation and does not establish interdomain orientation.
| Model | Origin | Core retention | Core mean pLDDT | Full mean pLDDT | Cautions |
|---|---|---|---|---|---|
| AF-A0A494C071-F1:v6 Canonical | GDM | complete | 79.9 | 50.2 | uncertain_protein_existence |
PWWP1 · Structural correspondence
Structural alignment establishes a residue correspondence for these cropped cores. It does not establish equivalent ligand pockets, function or selectivity.
| Domain pair | Aligned Cα | US-align RMSD Å | TM score A / B | View |
|---|---|---|---|---|
| No eligible experimental representative for a cross-domain comparison. | ||||