0 profiles
Deposited research ligands
No records in this category for the selected domain in the curated snapshot.
Protein record
Jasper
JIL-1 anchoring and stabilizing protein, isoform A
Drosophila melanogaster475 amino acidsannotation supported
1annotated core in Jasper
4PDB entries with observed PWWP1 coordinates
1model records for PWWP1
0frozen v1.2 assay / association records for PWWP1
Canonical sequence · Source-mapped regions
Protein domain architecture
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 coreOther source annotationPredicted candidate, when present
0 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.
Deposited construct mapping
1 selected exampleColored 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.
Mapping and construct evidence
Deposited polymer length: 85 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.
One mapped example per native domain, preferring frozen experimental representatives; up to four distinct mapped intervals.
Validated isoform differences · 0 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.
No source-validated alternative-isoform core mapping is available in this snapshot.
Viewing Jasper PWWP1
Canonical annotation interval 12–63 · UniProtKB DOMAIN. annotation core; not a certified complete folded domain or pocket.
Alternative PWWP annotations and interval provenance
No alternative annotation record is available in this snapshot.
PWWP1 · source-classified Phase 6A evidence
Ligands & Bioactivity
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.
1 profiles
Ambiguous / indirect evidence
Bis-Tris0 observations · 0 research-ligand entriesPWWP1 · Deposited coordinates
Experimental coverage and AlphaFold correspondence
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 |
|---|---|---|---|---|---|---|
| 6KCO | A | 52 / 52 | Complexes | X-RAY DIFFRACTION 2.4 Å | 0.617 | No classification flag |
| 6KCP | A | 52 / 52 | Complexes | X-RAY DIFFRACTION 1.8 Å | 0.588 | No classification flag |
| 6KCU | A | 52 / 52 | APO | X-RAY DIFFRACTION 1.65 Å | 0.42 | No classification flag |
| 6KD6 | B | 51 / 52 | APO | X-RAY DIFFRACTION 1.58 Å | 0.486 | No classification flag |
PWWP1 · Measured preparations
Frozen v1.2 assay records
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
Predicted models
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-Q9VAA9-F1:v6 Canonical | GDM | complete | 91.6 | 73.3 |
PWWP1 · Structural correspondence
Human annotation-core comparisons
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. | ||||