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1PT8

Crystal structure of the yfdW gene product of E. coli, in complex with oxalate and acetyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008410molecular_functionCoA-transferase activity
A0016740molecular_functiontransferase activity
A0033608molecular_functionformyl-CoA transferase activity
A0033611biological_processoxalate catabolic process
A0071468biological_processcellular response to acidic pH
B0003824molecular_functioncatalytic activity
B0008410molecular_functionCoA-transferase activity
B0016740molecular_functiontransferase activity
B0033608molecular_functionformyl-CoA transferase activity
B0033611biological_processoxalate catabolic process
B0071468biological_processcellular response to acidic pH
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXL B 801
ChainResidue
AGLN48
ALEU49
BGLY249
BHOH993

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OXL A 802
ChainResidue
AGLY249
BGLN48

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ACO A 751
ChainResidue
AARG38
ALEU72
ATHR74
ALYS75
AASN96
APHE97
AHIS98
AALA101
AILE124
ALYS137
AALA138
ATYR139
AGLU140
AASP169
AMET200
AHOH1129
AHOH1133
BGLY248
BGLY249
BGLN273
BGLN275
AVAL16
AGLN17
ASER18

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ACO B 752
ChainResidue
AGLY248
AGLY249
AGLN273
BVAL16
BGLN17
BSER18
BARG38
BLEU72
BTHR74
BLYS75
BASN96
BPHE97
BHIS98
BALA101
BILE124
BLYS137
BALA138
BTYR139
BGLU140
BASP169
BMET200
BHOH1077
BHOH1095
BHOH1109

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 901
ChainResidue
ATRP28
APRO381
AASP382

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
AGLU95
AASP103
APHE121
ASER123
AARG195

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 903
ChainResidue
AHOH951
BPHE155
BHOH937

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 904
ChainResidue
AARG50
APRO53
AHOH1032
BLEU221
BTYR223
BHOH1018

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 905
ChainResidue
BTRP28
BPRO381
BASP382

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12844490
ChainResidueDetails
AASP169
BASP169

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AGLN17
BGLN273
ALEU72
AASN96
ALYS137
AGLN273
BGLN17
BLEU72
BASN96
BLYS137

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:14993676
ChainResidueDetails
AARG38
BARG38

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00742
ChainResidueDetails
AHIS104
BHIS104

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLY248
BGLY248

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

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PDB entries from 2024-07-17

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