Structure of PDB 2y0m Chain A

Receptor sequence
>2y0mA (length=273) Species: 9606 (Homo sapiens) [Search protein sequence]
KYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFH
LGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTL
YFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRR
GYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF
RGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHL
KSAQYKKPPITVDSVCLKWAPPK
3D structure
PDB2y0m Structural Basis for Mof and Msl3 Recruitment Into the Dosage Compensation Complex by Msl1.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C316 E350
Catalytic site (residue number reindexed from 1) C140 E174
Enzyme Commision number 2.3.1.-
2.3.1.48: histone acetyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ACO A F270 L271 C316 I317 L318 T319 Q324 R325 G327 G329 K330 L353 S354 L356 S360 S363 K432 F94 L95 C140 I141 L142 T143 Q148 R149 G151 G153 K154 L177 S178 L180 S184 S187 K256
BS02 ZN A C210 C213 H226 C230 C34 C37 H50 C54
Gene Ontology
Molecular Function
GO:0004402 histone acetyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

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Molecular Function
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Biological Process
External links
PDB RCSB:2y0m, PDBe:2y0m, PDBj:2y0m
PDBsum2y0m
PubMed21217699
UniProtQ9H7Z6|KAT8_HUMAN Histone acetyltransferase KAT8 (Gene Name=KAT8)

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