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

Exact experimental source · Phase 6D

5NRV · 96K

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

Original structure and viewer
12Protein-chain contacts within 5 Å
16Protein-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:5NRV:LIG:C:96K:401:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
d069ff65539e46f88b81c09ce8b540b38d9403ad77689dc00093cd38d90162bf
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_only
Fingerprint
12 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
65SER2701542.579 ÅOG · O8
61ASP2661452.603 ÅOD2 · N1
64PHE2691533.431 ÅO · C7
31PHE236453.553 ÅCE1 · C12
34TRP239483.555 ÅCB · C11
58TRP2631423.650 ÅCG · C9
28ILE233323.722 ÅCD1 · C11
92SERUnmappedUnqualified3.740 ÅOG · C14
63LYS2681524.081 ÅCB · C5
32SER237464.796 ÅO · C11
46LYSUnmappedUnqualified4.956 ÅNZ · C7
66GLU2711554.966 ÅN · O8
26GLY231305.232 ÅO · C11
90LEUUnmappedUnqualified5.555 ÅCD1 · C14
59PHE2641435.713 ÅO · C9
93TYRUnmappedUnqualified5.851 ÅN · C14

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
28ILE233single / commonNoneNone
31PHE236single / commonNoneNone
34TRP239single / commonNoneNone
58TRP263single / commonNoneNone
61ASP266single / commonNoneNone
63LYS268single / commonNoneNone
64PHE269single / commonNoneNone
65SER270single / commonNoneNone

Compare experimental site geometry

Further comparisons

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