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3IT6

The Crystal Structure of Ornithine Acetyltransferase complexed with Ornithine from Mycobacterium tuberculosis (Rv1653) at 2.4 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
A0006526biological_processL-arginine biosynthetic process
B0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
B0006526biological_processL-arginine biosynthetic process
C0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
C0006526biological_processL-arginine biosynthetic process
D0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
D0006526biological_processL-arginine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ORN B 1
ChainResidue
ATHR166
BSER404
ALYS189
AGLY192
AMET193
AHOH381
BHOH102
BTHR200
BGLU280
BASN399

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ORN D 1
ChainResidue
BARG325
CTHR127
CTHR166
CLYS189
CGLY192
CMET193
DHOH77
DHOH80
DTHR200
DGLU280
DASN399
DSER404

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

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PDB entries from 2025-12-03

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