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

Exact experimental source · Phase 6D

5NV2 · 9AE

UP:Q9UBC3:PWWP1 · protein label chain A · ligand label chain C · model 1

Original structure and viewer
9Protein-chain contacts within 5 Å
13Protein-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:5NV2:LIG:C:9AE:401:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
90c69902789421dcb9c6982f74df193641fd6d84bf5163de125de814878ab7b1
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
61ASP2661452.931 ÅOD2 · C9
28ILE233323.521 ÅCG1 · C12
34TRP239483.691 ÅCH2 · C5
31PHE236453.763 ÅCG · C10
58TRP2631423.809 ÅCH2 · C11
92SERUnmappedUnqualified4.026 ÅCB · C8
63LYS2681524.597 ÅCD · C9
32SER237464.728 ÅO · C11
26GLY231304.804 ÅO · C11
65SER2701545.090 ÅOG · C12
60GLY2651445.519 ÅC · C8
27LYS232315.569 ÅC · C11
90LEUUnmappedUnqualified5.727 ÅCD1 · C5

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