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

Exact experimental source · Phase 6D

5NRS · 962

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

Original structure and viewer
10Protein-chain contacts within 5 Å
14Protein-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:5NRS:LIG:E:962:403:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
a9f3140c8fe61aee17ed09b3c67bc8a7bda6fe726e5e5eb80203676d4492f602
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_only
Fingerprint
13 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
61ASP2661452.969 ÅOD2 · C10
31PHE236453.064 ÅCE1 · O8
63LYS2681523.340 ÅCD · O12
58TRP2631423.619 ÅCD1 · C10
34TRP239483.656 ÅCB · O4
28ILE233323.787 ÅCB · O4
92SERUnmappedUnqualified4.392 ÅOG · C9
32SER237464.603 ÅO · O4
65SER2701544.632 ÅOG · O12
26GLY231304.660 ÅO · O4
27LYS232315.564 ÅC · O4
64PHE2691535.643 ÅO · O12
59PHE2641435.753 ÅO · C6
33TRP238475.978 ÅC · O4

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