3FGN
Crystal structure of dethiobiotin synthetase in Mycobacterium tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004141 | molecular_function | dethiobiotin synthase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009102 | biological_process | biotin biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004141 | molecular_function | dethiobiotin synthase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009102 | biological_process | biotin biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004141 | molecular_function | dethiobiotin synthase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0009102 | biological_process | biotin biosynthetic process |
C | 0016874 | molecular_function | ligase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004141 | molecular_function | dethiobiotin synthase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0009102 | biological_process | biotin biosynthetic process |
D | 0016874 | molecular_function | ligase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00336 |
Chain | Residue | Details |
A | LYS37 | |
B | LYS37 | |
C | LYS37 | |
D | LYS37 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: 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 |
Chain | Residue | Details |
C | THR11 | |
C | PRO197 | |
D | THR11 | |
D | PRO197 | |
A | THR11 | |
A | PRO197 | |
B | THR11 | |
B | PRO197 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | THR16 | |
A | ASP49 | |
A | GLU108 | |
B | THR16 | |
B | ASP49 | |
B | GLU108 | |
C | THR16 | |
C | ASP49 | |
C | GLU108 | |
D | THR16 | |
D | ASP49 | |
D | GLU108 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0000269|DOI:10.1021/acscatal.8b03475, ECO:0007744|PDB:3FMF, ECO:0007744|PDB:3FMI, ECO:0007744|PDB:6CVE |
Chain | Residue | Details |
A | LYS37 | |
B | LYS37 | |
C | LYS37 | |
D | LYS37 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00336 |
Chain | Residue | Details |
A | THR41 | |
B | THR41 | |
C | THR41 | |
D | THR41 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | GLY144 | |
B | GLY144 | |
C | GLY144 | |
D | GLY144 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | GLY169 | |
B | GLY169 | |
C | GLY169 | |
D | GLY169 |