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1ZFN

Structural Analysis of Escherichia coli ThiF

Functional Information from GO Data
ChainGOidnamespacecontents
A0004792molecular_functionthiosulfate 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
A0016779molecular_functionnucleotidyltransferase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0052837biological_processthiazole biosynthetic process
A0070733molecular_functionAMPylase activity
A1902503cellular_componentadenylyltransferase complex
A1990228cellular_componentsulfurtransferase complex
B0004792molecular_functionthiosulfate 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
B0016779molecular_functionnucleotidyltransferase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0052837biological_processthiazole biosynthetic process
B0070733molecular_functionAMPylase activity
B1902503cellular_componentadenylyltransferase complex
B1990228cellular_componentsulfurtransferase complex
C0004792molecular_functionthiosulfate 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
C0016779molecular_functionnucleotidyltransferase activity
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0052837biological_processthiazole biosynthetic process
C0070733molecular_functionAMPylase activity
C1902503cellular_componentadenylyltransferase complex
C1990228cellular_componentsulfurtransferase complex
D0004792molecular_functionthiosulfate 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
D0016779molecular_functionnucleotidyltransferase activity
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0052837biological_processthiazole biosynthetic process
D0070733molecular_functionAMPylase activity
D1902503cellular_componentadenylyltransferase complex
D1990228cellular_componentsulfurtransferase complex
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 Residues4
DetailsACT_SITE: Glycyl persulfide ester intermediate
ChainResidueDetails
ACYS184
BCYS184
CCYS184
DCYS184

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING:
ChainResidueDetails
AARG11
BASP59
BARG70
BLYS83
BLEU107
BASP127
CARG11
CGLY38
CASP59
CARG70
CLYS83
AGLY38
CLEU107
CASP127
DARG11
DGLY38
DASP59
DARG70
DLYS83
DLEU107
DASP127
AASP59
AARG70
ALYS83
ALEU107
AASP127
BARG11
BGLY38

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:16388576
ChainResidueDetails
ACYS169
CCYS172
CCYS240
CCYS243
DCYS169
DCYS172
DCYS240
DCYS243
ACYS172
ACYS240
ACYS243
BCYS169
BCYS172
BCYS240
BCYS243
CCYS169

site_idSWS_FT_FI4
Number of Residues8
DetailsCROSSLNK: Glycyl cysteine dithioester (Cys-Gly) (interchain with G-Cter in ThiS)
ChainResidueDetails
ACYS184
BCYS184
CCYS184
DCYS184

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PDB entries from 2024-09-18

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