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

Exact experimental source · Phase 6D

5NVO · CHT

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

Original structure and viewer
6Protein-chain contacts within 5 Å
10Protein-chain contacts within 6 Å
8Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:5NVO:LIG:J:CHT:401:.:SITE:UP:Q9UBC3:PWWP1:B
Original mmCIF SHA-256
2064abc26e049d5b45a8e32a53fa1536f42e4d3017076d719e8a29a5a6b4ae9c
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_only
Fingerprint
10 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.

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 residueResidueCanonical positionMSA columnMin. heavy-atom distanceContact atoms
61ASP2661452.637 ÅOD2 · O6
34TRP239483.373 ÅCD1 · C8
58TRP2631423.414 ÅCD1 · O6
31PHE236453.504 ÅCD1 · C7
63LYS2681524.183 ÅCB · O6
28ILE233324.289 ÅCD1 · C6
32SER237465.301 ÅO · C6
59PHE2641435.350 ÅO · C8
26GLY231305.415 ÅO · C6
65SER2701545.440 ÅOG · O6

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
28ILE233single / commonNoneNone
31PHE236single / commonNoneNone
34TRP239single / commonNoneNone
58TRP263single / commonNoneNone
59PHE264single / commonNoneNone
61ASP266single / commonNoneNone
63LYS268single / commonNoneNone
65SER270single / commonNoneNone

Compare experimental site geometry

Further comparisons

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