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

Exact experimental source · Phase 6D

5NRR · 96E

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

Original structure and viewer
10Protein-chain contacts within 5 Å
14Protein-chain contacts within 6 Å
5Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:5NRR:LIG:C:96E:401:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
ab09d824a29b987279f6178899a03ddb8e496509769ce2e3558b670c6826e1e0
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
92SERUnmappedUnqualified2.836 ÅOG · O13
61ASP2661453.106 ÅOD2 · C03
31PHE236453.449 ÅCE1 · C08
58TRP2631423.555 ÅCD1 · C02
34TRP239483.625 ÅCG · C06
28ILE233323.752 ÅCG1 · C07
63LYS2681523.914 ÅCD · C02
65SER2701544.203 ÅOG · O01
90LEUUnmappedUnqualified4.282 ÅCD1 · O13
32SER237464.619 ÅO · C07
26GLY231305.011 ÅO · C07
64PHE2691535.632 ÅO · O01
27LYS232315.820 ÅC · C07
93TYRUnmappedUnqualified5.848 ÅN · O13

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
31PHE236single / commonNoneNone
34TRP239single / commonNoneNone
58TRP263single / 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