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

Exact experimental source · Phase 6D

5NV7 · 9AK

UP:Q9UBC3:PWWP1 · protein label chain B · ligand label chain F · model 1

Original structure and viewer
7Protein-chain contacts within 5 Å
12Protein-chain contacts within 6 Å
6Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:5NV7:LIG:F:9AK:401:.:SITE:UP:Q9UBC3:PWWP1:B
Original mmCIF SHA-256
ab98f5d00f60fe78b9b0cc391381b550dca1ff8f496b469a7bc4dab2c5e66875
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_only
Fingerprint
11 qualified aligned contact positions
View original Phase 6C.1 ligand environment

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.

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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 residueResidueCanonical positionMSA columnMin. heavy-atom distanceContact atoms
34TRP239483.413 ÅCD1 · C5
58TRP2631423.443 ÅCG · C5
61ASP2661453.454 ÅOD2 · N1
92SERUnmappedUnqualified3.932 ÅCB · O9
31PHE236454.001 ÅCE2 · C2
28ILE233324.638 ÅCD1 · N4
59PHE2641434.892 ÅO · C5
63LYS2681525.589 ÅCD · C6
65SER2701545.793 ÅOG · C6
32SER237465.842 ÅO · N4
35PRO240495.923 ÅO · C5
60GLY2651445.977 ÅC · O9

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
31PHE236single / commonNoneNone
34TRP239single / commonNoneNone
58TRP263single / commonNoneNone
59PHE264single / commonNoneNone
61ASP266single / commonNoneNone
63LYS268single / commonNoneNone
92SER—single / commonNoneNone

Compare experimental site geometry

Further comparisons

All research-ligand observations for this domain · Original structural quality · Chemical classifications and assays