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6MTG

A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein Structure

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 PEG A 401
ChainResidue
AALA82
AHOH561
BLEU152
BTYR153
BGLY154

site_idAC2
Number of Residues11
Detailsbinding site for residue PEG A 402
ChainResidue
AHOH548
AHOH564
AHOH704
BARG56
BSER59
BASN60
BHOH604
AGLU18
AVAL20
AHIS176
AARG181

site_idAC3
Number of Residues5
Detailsbinding site for residue FMT A 403
ChainResidue
AALA177
ALEU178
ALEU179
ATYR292
AHOH624

site_idAC4
Number of Residues5
Detailsbinding site for residue FMT A 404
ChainResidue
ALEU255
AASP256
AHOH513
BLYS47
BARG78

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL B 401
ChainResidue
BLEU173
BHIS174
BGLU209
BILE210

site_idAC6
Number of Residues5
Detailsbinding site for residue FMT B 402
ChainResidue
BALA177
BLEU178
BLEU179
BTYR292
BHOH555

site_idAC7
Number of Residues6
Detailsbinding site for residue FMT B 403
ChainResidue
BGLY107
BALA108
BCSD142
BTRP143
BHIS235
BHOH591

site_idAC8
Number of Residues3
Detailsbinding site for residue FMT B 404
ChainResidue
AGLN158
BGLU8
BASP117

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

248335

PDB entries from 2026-01-28

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