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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
A0008652biological_processamino acid biosynthetic process
A0008899molecular_functionhomoserine O-succinyltransferase activity
A0009086biological_processmethionine biosynthetic process
A0016740molecular_functiontransferase activity
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
B0008652biological_processamino acid biosynthetic process
B0008899molecular_functionhomoserine O-succinyltransferase activity
B0009086biological_processmethionine biosynthetic process
B0016740molecular_functiontransferase activity
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
DetailsActive site: {"description":"Acyl-thioester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10572016","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17302437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17442255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17302437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17442255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17302437","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17442255","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for acyl-CoA specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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