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1ZUD

Structure of ThiS-ThiF protein complex

Functional Information from GO Data
ChainGOidnamespacecontents
10000166molecular_functionnucleotide binding
10004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
10005524molecular_functionATP binding
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10008146molecular_functionsulfotransferase activity
10008270molecular_functionzinc ion binding
10008641molecular_functionubiquitin-like modifier activating enzyme activity
10009228biological_processthiamine biosynthetic process
10009229biological_processthiamine diphosphate biosynthetic process
10016740molecular_functiontransferase activity
10016779molecular_functionnucleotidyltransferase activity
10042803molecular_functionprotein homodimerization activity
10046872molecular_functionmetal ion binding
10052837biological_processthiazole biosynthetic process
10070733molecular_functionAMPylase activity
20000166molecular_functionnucleotide binding
20009228biological_processthiamine biosynthetic process
20009229biological_processthiamine diphosphate biosynthetic process
20052837biological_processthiazole biosynthetic process
20097163molecular_functionsulfur carrier activity
21902503cellular_componentadenylyltransferase complex
30000166molecular_functionnucleotide binding
30004792molecular_functionthiosulfate-cyanide sulfurtransferase activity
30005524molecular_functionATP binding
30005737cellular_componentcytoplasm
30005829cellular_componentcytosol
30008146molecular_functionsulfotransferase activity
30008270molecular_functionzinc ion binding
30008641molecular_functionubiquitin-like modifier activating enzyme activity
30009228biological_processthiamine biosynthetic process
30009229biological_processthiamine diphosphate biosynthetic process
30016740molecular_functiontransferase activity
30016779molecular_functionnucleotidyltransferase activity
30042803molecular_functionprotein homodimerization activity
30046872molecular_functionmetal ion binding
30052837biological_processthiazole biosynthetic process
30070733molecular_functionAMPylase activity
40000166molecular_functionnucleotide binding
40009228biological_processthiamine biosynthetic process
40009229biological_processthiamine diphosphate biosynthetic process
40052837biological_processthiazole biosynthetic process
40097163molecular_functionsulfur carrier activity
41902503cellular_componentadenylyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN 1 501
ChainResidue
1CYS169
1CYS172
1CYS240
1CYS243

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN 3 502
ChainResidue
3CYS169
3CYS172
3CYS240
3CYS243

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA 3 601
ChainResidue
1ASP16
1HOH704
3LEU14
3ASP16
3HOH764
1LEU14

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA 1 602
ChainResidue
1CYS243
1HOH800
1HOH801
1HOH802
3HOH772
3HOH809
3HOH810

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA 1 701
ChainResidue
1VAL116
1ALA117
1ALA119
1THR144
1HOH755
1HOH757

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA 3 702
ChainResidue
3VAL116
3ALA117
3ALA119
3THR144
3HOH796
3HOH808

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16388576","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Glycyl adenylate; alternate","evidences":[{"source":"PubMed","id":"9632726","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsCross-link: {"description":"Glycyl cysteine dithioester (Gly-Cys) (interchain with C-184 in ThiF); alternate"}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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