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2H2W

Crystal structure of Homoserine O-succinyltransferase (EC 2.3.1.46) (Homoserine O-transsuccinylase) (HTS) (tm0881) from THERMOTOGA MARITIMA at 2.52 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 SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
ACYS142

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
AHIS234

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
AGLU236

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
ALYS163
ASER191
AARG248

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
ASER191

227344

PDB entries from 2024-11-13

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