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2IL4

Crystal structure of At1g77540-Coenzyme A Complex

Replaces:  2GDB
Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0008150biological_processbiological_process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE COA A 104
ChainResidue
AHIS22
ALEU53
AALA54
ASER55
ASER66
ACYS76
ASER77
ATYR78
ATHR82
AARG86
ASER89
AHIS41
ATRP90
AHOH105
AHOH112
AHOH120
AHOH143
AHOH152
AHOH161
ATHR42
ATYR43
AVAL44
AARG49
AGLY50
ALEU51
AGLY52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17128971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17850744","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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