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

Exact experimental source · Phase 6D

7HHP · A1A3Z

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

Original structure and viewer
8Protein-chain contacts within 5 Å
14Protein-chain contacts within 6 Å
8Qualified local alignment positions
0Side-chain incomplete residues in local neighborhood

Identity and provenance

Source evidence
phase6a:site_classification:PDB:7HHP:LIG:J:A1A3Z:103:.:SITE:UP:Q7Z4V5:PWWP1:B
Original mmCIF SHA-256
1c3b7d67c238bf0ad23d5d162842759e923a577a117f31d72b899460a8a4fe66
Experimental method
'X-RAY DIFFRACTION'
Source site class
deposited_research_ligand · source_observed
Assembly context
asymmetric_unit_multi_chain_possible
Fingerprint
13 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
48THR471452.616 ÅOG1 · O
50GLU491522.723 ÅOE1 · O
51THR501533.172 ÅO · C7
16MET15323.282 ÅCG · C3
22TRP21483.517 ÅCZ3 · C
45PHE441423.528 ÅCE2 · C3
19TYR18453.554 ÅOH · C11
52ALA511544.041 ÅCB · C7
76LYSUnmappedUnqualified5.078 ÅO · C
14ALA13305.099 ÅO · C3
20PRO19465.206 ÅO · C3
49HIS481465.554 ÅN · O
15LYS14315.773 ÅC · C3
46PHE451435.943 ÅO · C1

Local atomic completeness

Label residueTypeCanonicalObserved conformerMissing backboneMissing side chain
16MET15single / commonNoneNone
19TYR18single / commonNoneNone
22TRP21single / commonNoneNone
45PHE44single / commonNoneNone
48THR47single / commonNoneNone
50GLU49single / commonNoneNone
51THR50single / commonNoneNone
52ALA51single / commonNoneNone

Compare experimental site geometry

Further comparisons

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