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

Exact experimental source · Phase 6D

6UE6 · Q5D

UP:O96028:PWWP1 · protein label chain G · ligand label chain UA · model 1

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

Identity and provenance

Source evidence
phase6a:site_classification:PDB:6UE6:LIG:UA:Q5D:2001:.:SITE:UP:O96028:PWWP1:G
Original mmCIF SHA-256
fbf22f430937d8ed0ad110294f251af23fd33f7e8bf3164fe0dc9e3cb4f21d27
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_multi_chain_possible
Fingerprint
1 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.

Original coordinate file has not been loaded into this browser.

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
108LYSUnmappedUnqualified3.569 ÅCD · O
111ALAUnmappedUnqualified3.589 ÅCB · C14
60ASP2691453.872 ÅOD2 · C15
112GLNUnmappedUnqualified4.199 ÅCG · C15
107GLYUnmappedUnqualified4.968 ÅO · C13
109LEUUnmappedUnqualified5.944 ÅN · C13

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
108LYS—single / commonNoneNone

Compare experimental site geometry

Further comparisons

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