6CZC
Crystal structure of Mycobacterium tuberculosis dethiobiotin synthetase in complex with thymidine triphosphate (TTP) - promiscuous binding mode with disordered nucleoside
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 PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue MG A 301 |
Chain | Residue |
A | THR16 |
A | ASP49 |
A | GLU108 |
A | TTP302 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue TTP A 302 |
Chain | Residue |
A | THR16 |
A | VAL17 |
A | LYS37 |
A | ASP49 |
A | GLU52 |
A | GLU108 |
A | GLY111 |
A | MG301 |
A | HOH402 |
A | HOH406 |
A | HOH414 |
A | HOH429 |
A | HOH497 |
A | HOH514 |
A | THR11 |
A | GLY12 |
A | VAL13 |
A | GLY14 |
A | LYS15 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG B 301 |
Chain | Residue |
B | THR16 |
B | LYS37 |
B | ASP49 |
B | GLU108 |
B | TTP302 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue TTP B 302 |
Chain | Residue |
B | GLY12 |
B | VAL13 |
B | GLY14 |
B | LYS15 |
B | THR16 |
B | VAL17 |
B | LYS37 |
B | ASP49 |
B | GLU108 |
B | ALA110 |
B | GLY111 |
B | MG301 |
B | HOH408 |
B | HOH448 |
B | HOH518 |
B | HOH557 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MG C 301 |
Chain | Residue |
C | THR16 |
C | LYS37 |
C | ASP49 |
C | GLU108 |
C | TTP302 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for residue TTP C 302 |
Chain | Residue |
C | THR11 |
C | GLY12 |
C | VAL13 |
C | GLY14 |
C | LYS15 |
C | THR16 |
C | VAL17 |
C | LYS37 |
C | ASP49 |
C | GLU108 |
C | GLY111 |
C | MG301 |
C | HOH428 |
C | HOH449 |
C | HOH499 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG D 301 |
Chain | Residue |
D | THR16 |
D | ASP49 |
D | GLU108 |
D | TTP302 |
D | HOH408 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for residue TTP D 302 |
Chain | Residue |
D | THR11 |
D | GLY12 |
D | VAL13 |
D | GLY14 |
D | LYS15 |
D | THR16 |
D | LYS37 |
D | ASP49 |
D | GLU108 |
D | GLY111 |
D | MG301 |
D | HOH402 |
D | HOH403 |
D | HOH408 |
D | HOH473 |
D | HOH521 |
D | HOH524 |
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 |
D | THR41 | |
A | THR41 | |
B | THR41 | |
C | 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 |
D | GLY144 | |
A | GLY144 | |
B | GLY144 | |
C | 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 |