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

Exact experimental source · Phase 6D

9Y60 · A1CSP

UP:O96028:PWWP1 · protein label chain A · ligand label chain B · model 1

Original structure and viewer
14Protein-chain contacts within 5 Å
16Protein-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:9Y60:LIG:B:A1CSP:4000:.:SITE:UP:O96028:PWWP1:A
Original mmCIF SHA-256
9ef0f36f9163b9d77a33b0955701d6fc233d3a9e69ec6c18caa65da3ed3e1df2
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
70ALA2701462.883 ÅN · O1
121GLNUnmappedUnqualified2.894 ÅOE1 · N1
36TRP236483.298 ÅCZ2 · N1
66PHE2661423.308 ÅCB · O2
69ASP2691453.330 ÅN · O1
68GLY2681443.343 ÅCA · O1
33TYR233453.406 ÅCB · CL2
72GLU2721523.545 ÅCG · C1
67PHE2671433.574 ÅO · C8
30VAL230323.758 ÅCG2 · CL2
118LEUUnmappedUnqualified3.768 ÅCD1 · C9
34PRO234464.439 ÅO · CL2
71PROUnmappedUnqualified4.474 ÅN · O1
28SER228304.726 ÅO · CL2
122TRPUnmappedUnqualified5.437 ÅN · N1
29LYS229315.802 ÅC · CL2

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
118LEU—single / commonNoneNone
121GLN—single / commonNoneNone
33TYR233single / commonNoneNone
36TRP236single / commonNoneNone
66PHE266single / commonNoneNone
67PHE267single / commonNoneNone
70ALA270single / commonNoneNone
71PRO—single / commonNoneNone
72GLU272single / commonNoneNone

Compare experimental site geometry

Further comparisons

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