Crystal structure of human GCN5 histone acetyltransferase domain
Lu, X.T., Tao, Y.J.To be published.
Experimental Data Snapshot
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Histone acetyltransferase KAT2A | 165 | Homo sapiens | Mutation(s): 0  Gene Names: KAT2A, GCN5, GCN5L2 EC: 2.3.1.48 (PDB Primary Data), 2.3.1 (PDB Primary Data) | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q92830 (Homo sapiens) Explore Q92830  Go to UniProtKB:  Q92830 | |||||
PHAROS:  Q92830 GTEx:  ENSG00000108773  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q92830 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 1 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
UQ3 (Subject of Investigation/LOI) Query on UQ3 | D [auth A], E [auth B], F [auth C] | S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5,10,14-tetraoxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} (2R)-2-hydroxypropanethioate C24 H40 N7 O18 P3 S VIWKEBOLLIEAIL-AGCMQPJKSA-N |
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 137.889 | α = 90 |
b = 137.889 | β = 90 |
c = 154.875 | γ = 90 |
Software Name | Purpose |
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PHENIX | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
PHENIX | phasing |
Funding Organization | Location | Grant Number |
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Robert A. Welch Foundation | United States | C-1565 |