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1PT5

Crystal structure of gene yfdW of E. coli

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 Residues29
DetailsBINDING SITE FOR RESIDUE ACO A 901
ChainResidue
AVAL16
APHE97
AHIS98
AALA101
AILE124
ALYS137
AALA138
ATYR139
AGLU140
AASP169
AMET200
AGLN17
AHOH974
AHOH1039
AHOH1047
AHOH1179
AHOH1186
AHOH1196
BGLY248
BGLY249
BGLN273
BGLN275
ASER18
AARG38
ALEU72
AASN73
ATHR74
ALYS75
AASN96

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE ACO B 801
ChainResidue
AGLY248
AGLY249
AGLN273
BPHE13
BVAL16
BGLN17
BSER18
BARG38
BLEU72
BASN73
BTHR74
BLYS75
BASN96
BPHE97
BHIS98
BALA101
BILE124
BLYS137
BALA138
BTYR139
BGLU140
BASP169
BMET200
BHOH858
BHOH931
BHOH935
BHOH954
BHOH981
BHOH1055

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
AASN96
ALYS137
AGLN273
BGLN17
BLEU72
BASN96
BLYS137
BGLN273
AGLN17
ALEU72

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

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PDB entries from 2024-04-17

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