Exact experimental source · Phase 6D
5NR3 · 95E
UP:Q9UBC3:PWWP1 · protein label chain B · ligand label chain G · model 1
Identity and provenance
- Source evidence
- phase6a:site_classification:PDB:5NR3:LIG:G:95E:401:.:SITE:UP:Q9UBC3:PWWP1:B
- Original mmCIF SHA-256
- 44a1bc37a1ec9502897975301189695e250abc526861869774ca6a1d0adc0dab
- Experimental method
- 'X-RAY DIFFRACTION'
- Source site class
- deposited_research_ligand · source_observed
- Assembly context
- asymmetric_unit_only
- Fingerprint
- 10 qualified aligned contact positions
Original experimental coordinates
Load the exact deposited source bytes; the browser verifies the original SHA-256 before drawing. Contacting protein residues and the specified ligand are highlighted only where the local parser can uniquely match source chain and residue identifiers. Otherwise the unmodified deposited structure remains available without an invented interaction highlight.
Original coordinate file has not been loaded into this browser.
Measured residue contacts
The table shows deposited protein-chain residue geometry, including native sequence identifiers. The listed contact atoms are selected under explicit alternate-conformer policy.
| Label residue | Residue | Canonical position | MSA column | Min. heavy-atom distance | Contact atoms |
|---|---|---|---|---|---|
| 61 | ASP | 266 | 145 | 2.654 Å | OD2 · O1 |
| 58 | TRP | 263 | 142 | 3.342 Å | CG · C2 |
| 34 | TRP | 239 | 48 | 3.437 Å | CD2 · C4 |
| 92 | SER | Unmapped | Unqualified | 3.442 Å | OG · C10 |
| 31 | PHE | 236 | 45 | 3.880 Å | CD1 · C4 |
| 28 | ILE | 233 | 32 | 4.171 Å | CG1 · C5 |
| 90 | LEU | Unmapped | Unqualified | 4.271 Å | CD1 · C14 |
| 63 | LYS | 268 | 152 | 4.420 Å | CD · O1 |
| 26 | GLY | 231 | 30 | 5.356 Å | O · C5 |
| 32 | SER | 237 | 46 | 5.372 Å | O · C5 |
| 65 | SER | 270 | 154 | 5.586 Å | OG · O1 |
| 59 | PHE | 264 | 143 | 5.601 Å | O · C7 |
Local atomic completeness
| Label residue | Type | Canonical | Observed conformer | Missing backbone | Missing side chain |
|---|---|---|---|---|---|
| 31 | PHE | 236 | single / common | None | None |
| 34 | TRP | 239 | single / common | None | None |
| 58 | TRP | 263 | single / common | None | None |
| 59 | PHE | 264 | single / common | None | None |
| 61 | ASP | 266 | single / common | None | None |
| 63 | LYS | 268 | single / common | None | None |
| 90 | LEU | — | single / common | None | None |
| 92 | SER | — | single / common | None | None |
| 93 | TYR | — | single / common | None | None |
Compare experimental site geometry
Further comparisons
All research-ligand observations for this domain · Original structural quality · Chemical classifications and assays