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3FGN

Crystal structure of dethiobiotin synthetase in Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004141molecular_functiondethiobiotin synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009102biological_processbiotin biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004141molecular_functiondethiobiotin synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009102biological_processbiotin biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004141molecular_functiondethiobiotin synthase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009102biological_processbiotin biosynthetic process
C0016874molecular_functionligase activity
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004141molecular_functiondethiobiotin synthase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009102biological_processbiotin biosynthetic process
D0016874molecular_functionligase activity
D0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00336
ChainResidueDetails
ALYS37
BLYS37
CLYS37
DLYS37

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:25801336, ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:4WOP, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
CTHR11
CPRO197
DTHR11
DPRO197
ATHR11
APRO197
BTHR11
BPRO197

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:20565114, ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FPA, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6CVV, ECO:0007744|PDB:6CZB, ECO:0007744|PDB:6CZC, ECO:0007744|PDB:6CZD, ECO:0007744|PDB:6CZE, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
ATHR16
AASP49
AGLU108
BTHR16
BASP49
BGLU108
CTHR16
CASP49
CGLU108
DTHR16
DASP49
DGLU108

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:6CVE
ChainResidueDetails
ALYS37
BLYS37
CLYS37
DLYS37

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336
ChainResidueDetails
ATHR41
BTHR41
CTHR41
DTHR41

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:3FPA, ECO:0007744|PDB:6CVE
ChainResidueDetails
AGLY144
BGLY144
CGLY144
DGLY144

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:30289406, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:6CVE, ECO:0007744|PDB:6CVF, ECO:0007744|PDB:6CVU, ECO:0007744|PDB:6E05, ECO:0007744|PDB:6E06
ChainResidueDetails
AGLY169
BGLY169
CGLY169
DGLY169

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PDB entries from 2024-05-15

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