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

Exact experimental source · Phase 6D

5NV0 · 9AH

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

Original structure and viewer
9Protein-chain contacts within 5 Å
14Protein-chain contacts within 6 Å
7Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:5NV0:LIG:C:9AH:401:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
22acb380ed92e41a32434c5fca7f97c6ac12d30f80023a184e6f74d1dfff3729
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
61ASP2661452.926 ÅOD2 · C10
34TRP239483.235 ÅCG · C8
31PHE236453.322 ÅCE1 · N6
58TRP2631423.425 ÅCG · C7
28ILE233323.428 ÅCD1 · C9
92SERUnmappedUnqualified3.625 ÅOG · C5
63LYS2681523.870 ÅCD · C12
90LEUUnmappedUnqualified3.908 ÅCD1 · N6
65SER2701544.422 ÅOG · C12
32SER237465.014 ÅO · C9
64PHE2691535.505 ÅO · C12
26GLY231305.568 ÅO · C9
59PHE2641435.838 ÅO · C2
93TYRUnmappedUnqualified5.948 ÅN · C5

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
28ILE233single / commonNoneNone
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