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1ZFN

Structural Analysis of Escherichia coli ThiF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008146molecular_functionsulfotransferase activity
A0008270molecular_functionzinc ion binding
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0009228biological_processthiamine biosynthetic process
A0009229biological_processthiamine diphosphate biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0052837biological_processthiazole biosynthetic process
A0070733molecular_functionAMPylase activity
B0000166molecular_functionnucleotide binding
B0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008146molecular_functionsulfotransferase activity
B0008270molecular_functionzinc ion binding
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0009228biological_processthiamine biosynthetic process
B0009229biological_processthiamine diphosphate biosynthetic process
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0052837biological_processthiazole biosynthetic process
B0070733molecular_functionAMPylase activity
C0000166molecular_functionnucleotide binding
C0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0008146molecular_functionsulfotransferase activity
C0008270molecular_functionzinc ion binding
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0009228biological_processthiamine biosynthetic process
C0009229biological_processthiamine diphosphate biosynthetic process
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0052837biological_processthiazole biosynthetic process
C0070733molecular_functionAMPylase activity
D0000166molecular_functionnucleotide binding
D0004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0008146molecular_functionsulfotransferase activity
D0008270molecular_functionzinc ion binding
D0008641molecular_functionubiquitin-like modifier activating enzyme activity
D0009228biological_processthiamine biosynthetic process
D0009229biological_processthiamine diphosphate biosynthetic process
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0052837biological_processthiazole biosynthetic process
D0070733molecular_functionAMPylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 252
ChainResidue
ACYS169
ACYS172
ACYS240
ACYS243

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 252
ChainResidue
BCYS169
BCYS172
BCYS240
BVAL242
BCYS243

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 345
ChainResidue
CCYS169
CCYS172
CCYS240
CCYS243

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 445
ChainResidue
DCYS169
DCYS172
DCYS240
DCYS243

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP C 346
ChainResidue
CILE34
CGLY35
CGLY37
CGLY38
CASP59
CASP61
CSER66
CASN67
CARG70
CGLN71
CLYS83
CARG106
CLEU107
CCYS125
CTHR126
CASP127
CTHR131
DARG11

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP D 446
ChainResidue
CARG11
DILE34
DGLY35
DGLY37
DGLY38
DALA58
DASP59
DASP61
DSER66
DASN67
DARG70
DGLN71
DLYS83
DARG106
DLEU107
DCYS125
DTHR126
DASP127
DTHR131

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 253
ChainResidue
AILE34
AGLY35
AGLY37
AGLY38
AASP59
AASP61
AARG70
AGLN71
ALYS83
AGLN105
AARG106
ALEU107
ACYS125
ATHR126
AASP127
ATHR131
BARG11

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B 253
ChainResidue
AARG11
BGLY35
BGLY37
BGLY38
BASP59
BASP61
BSER66
BASN67
BARG70
BGLN71
BLYS83
BGLN105
BARG106
BLEU107
BCYS125
BTHR126
BASP127
BTHR131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Glycyl persulfide ester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16388576","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS)"}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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