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2VJL

Formyl-CoA transferase with aspartyl-CoA thioester intermediate derived from formyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0008410molecular_functionCoA-transferase activity
A0016740molecular_functiontransferase activity
A0033608molecular_functionformyl-CoA transferase activity
A0033611biological_processoxalate catabolic process
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0008410molecular_functionCoA-transferase activity
B0016740molecular_functiontransferase activity
B0033608molecular_functionformyl-CoA transferase activity
B0033611biological_processoxalate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE COA A1169
ChainResidue
AHIS15
AMET105
AVAL124
ALYS137
AVAL138
ATYR139
AASP169
AMET200
AHOH2115
AHOH2137
AHOH2138
AALA18
AARG38
ALEU72
AMET74
AASN96
APHE97
AGLY98
AARG104

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A3000
ChainResidue
AGLN17
APHE63
AALA166
AASP169
ASER170

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A4000
ChainResidue
AASP294
AASP297
AHOH2245
AHOH2294
AHOH2363

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A4001
ChainResidue
AGLY222
APHE245
AILE248
AHOH2161
AHOH2168
AHOH2198

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE COA B1169
ChainResidue
ALYS52
AGLY260
AHOH2219
BHIS15
BVAL16
BGLN17
BARG38
BLEU72
BASP73
BMET74
BLYS75
BPHE97
BGLY98
BARG104
BMET105
BTYR139
BGLU140
BASP169
BHOH2016
BHOH2160
BHOH2161
BHOH2162
BHOH2163
BHOH2164
BHOH2165
BCL3001

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B3000
ChainResidue
BGLN17
BALA18
BASP169
BHOH2096

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B3001
ChainResidue
AGLY261
AGLN262
AHOH2024
BTYR139
BCOA1169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:15213226
ChainResidueDetails
AASP169
BASP169

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AHIS15
BGLY260
ALEU72
AASN96
ALYS137
AGLY260
BHIS15
BLEU72
BASN96
BLYS137

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:12839984, ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462
ChainResidueDetails
AARG38
AARG104
BARG38
BARG104

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
AASP169

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xvt
ChainResidueDetails
BASP169

site_idMCSA1
Number of Residues5
DetailsM-CSA 155
ChainResidueDetails
AGLN17electrostatic stabiliser, hydrogen bond donor
AGLU140electrostatic stabiliser, hydrogen bond donor
AASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile
AGLY260electrostatic stabiliser, hydrogen bond acceptor
AGLY261electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 155
ChainResidueDetails
BGLN17electrostatic stabiliser, hydrogen bond donor
BGLU140electrostatic stabiliser, hydrogen bond donor
BASP169covalently attached, electrofuge, electrophile, nucleofuge, nucleophile
BGLY260electrostatic stabiliser, hydrogen bond acceptor
BGLY261electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-10-09

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