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7CBE

Crystal structure of Homoserine O-succinyltransferase from Escherichia coli K-12

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
A0042803molecular_functionprotein homodimerization activity
B0004414molecular_functionhomoserine O-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0008899molecular_functionhomoserine O-succinyltransferase activity
B0009086biological_processmethionine biosynthetic process
B0016746molecular_functionacyltransferase activity
B0019281biological_processL-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 401
ChainResidue
AHIS174
APRO175
AHIS176
AALA177
AHOH520

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 402
ChainResidue
BGLU18
BVAL20
BARG181
BHOH525
AARG56
AASN60
AHOH510
AHOH532

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL B 401
ChainResidue
BLEU110
BGLY111
BARG193
BTYR194
BALA195

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 402
ChainResidue
BASN116
BHIS174
BPRO175
BHIS176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:10572016, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255
ChainResidueDetails
ACYS142
BCYS142

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255
ChainResidueDetails
AHIS235
BHIS235

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255
ChainResidueDetails
AGLU237
BGLU237

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
ALYS163
ASER192
AARG249
BLYS163
BSER192
BARG249

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for acyl-CoA specificity => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
AGLY111
BGLY111

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_00295
ChainResidueDetails
ASER192
BSER192

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PDB entries from 2024-07-17

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