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2GHR

Crystal structure of homoserine o-succinyltransferase (NP_981826.1) from Bacillus cereus ATCC 10987 at 2.40 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004414molecular_functionhomoserine O-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0008899molecular_functionhomoserine O-succinyltransferase activity
A0009086biological_processmethionine biosynthetic process
A0016746molecular_functionacyltransferase activity
A0019281biological_processL-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ASER239
ACYS240
AARG278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013
ChainResidueDetails
ACYS142

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013
ChainResidueDetails
AHIS235

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013
ChainResidueDetails
AGLU237

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:18216013, ECO:0007744|PDB:2VDJ
ChainResidueDetails
ALYS163
ASER192
AARG249

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for acyl-CoA specificity => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
AGLU111

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
ASER192

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qdl
ChainResidueDetails
ACYS142
AGLU237
AHIS235

224201

PDB entries from 2024-08-28

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