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

Exact experimental source · Phase 6D

7HH7 · LJR

UP:Q7Z4V5:PWWP1 · protein label chain A · ligand label chain J · model 1

Original structure and viewer
2Protein-chain contacts within 5 Å
3Protein-chain contacts within 6 Å
2Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:7HH7:LIG:J:LJR:103:.:SITE:UP:Q7Z4V5:PWWP1:A
Original mmCIF SHA-256
75ad16da3ae3ec45d91de34931ff783417cebbf9a1d2753d969d1e97ee851ba5
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_multi_chain_possible
Fingerprint
2 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
32GLY31583.194 ÅCA · O2
31ASP30573.843 ÅO · O2
33ALAUnmappedUnqualified5.496 ÅN · O2

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
31ASP30single / commonNoneNone
32GLY31single / commonNoneNone

Compare experimental site geometry

Further comparisons

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