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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
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:10572016, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255
ChainResidueDetails
ACSD142
BCSD142

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

218853

PDB entries from 2024-04-24

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