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

Exact experimental source · Phase 6D

6R3E · 96H

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

Original structure and viewer
8Protein-chain contacts within 5 Å
14Protein-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:6R3E:LIG:C:96H:501:.:SITE:UP:Q9UBC3:PWWP1:A
Original mmCIF SHA-256
f11f4e7bcd8a67152407442feee80117e2f1d3146e35bbce7e8eacb39e404552
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
52ASP2661452.377 ÅOD2 · O13
25TRP239483.319 ÅNE1 · C12
49TRP2631423.355 ÅCD2 · C03
22PHE236453.441 ÅCE1 · C06
19ILE233323.970 ÅCG1 · O01
50PHE2641434.615 ÅO · C12
23SER237464.951 ÅO · O01
83SERUnmappedUnqualified4.993 ÅCB · C12
54LYS2681525.135 ÅNZ · O13
51GLY2651445.357 ÅC · C12
17GLY231305.472 ÅO · O01
87ALAUnmappedUnqualified5.562 ÅCB · C12
26PRO240495.791 ÅO · C03
56SER2701545.835 ÅOG · C02

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
19ILE233single / commonNoneNone
22PHE236single / commonNoneNone
25TRP239single / commonNoneNone
49TRP263single / commonNoneNone
52ASP266single / commonNoneNone
54LYS268single / commonNoneNone

Compare experimental site geometry

Further comparisons

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