4YPO
Crystal structure of Mycobacterium tuberculosis ketol-acid reductoisomerase in complex with Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004455 | molecular_function | ketol-acid reductoisomerase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP188 |
| A | GLU192 |
| A | HOH572 |
| A | HOH734 |
| A | HOH757 |
| B | HOH715 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH576 |
| A | HOH588 |
| A | HOH962 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | HOH559 |
| A | HOH642 |
| A | HOH699 |
| A | HOH872 |
| A | HOH888 |
| A | HOH973 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | HOH606 |
| A | HOH611 |
| A | HOH613 |
| A | HOH721 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | SER24 |
| A | GLN25 |
| A | PRO130 |
| A | GLY131 |
| A | HOH934 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 406 |
| Chain | Residue |
| A | GLU224 |
| A | GLU228 |
| A | HOH539 |
| A | HOH658 |
| B | ASP188 |
| B | HOH609 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 407 |
| Chain | Residue |
| A | ASP250 |
| A | HOH513 |
| A | HOH552 |
| A | HOH592 |
| A | HOH795 |
| B | HOH632 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 408 |
| Chain | Residue |
| A | ASP62 |
| A | HOH511 |
| A | HOH515 |
| A | HOH582 |
| A | HOH737 |
| B | HOH779 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 409 |
| Chain | Residue |
| A | SER323 |
| A | HOH612 |
| B | GLY143 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 410 |
| Chain | Residue |
| A | ASP188 |
| A | HOH573 |
| B | GLU224 |
| B | GLU228 |
| B | HOH544 |
| B | HOH687 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| A | HOH517 |
| A | HOH530 |
| A | HOH906 |
| B | HOH678 |
| B | HOH813 |
| B | HOH850 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP188 |
| B | GLU192 |
| B | HOH576 |
| B | HOH742 |
| B | HOH747 |
| B | HOH760 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASP60 |
| B | HOH549 |
| B | HOH554 |
| B | HOH702 |
| B | HOH764 |
| B | HOH811 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | HOH708 |
| B | HOH861 |
| B | HOH871 |
| B | HOH880 |
| B | HOH908 |
| B | HOH931 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 405 |
| Chain | Residue |
| A | HOH971 |
| B | HOH537 |
| B | HOH585 |
| B | HOH593 |
| B | HOH712 |
| B | HOH895 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 406 |
| Chain | Residue |
| B | ALA68 |
| B | ALA71 |
| B | ASN94 |
| B | LYS96 |
| B | ASP99 |
| B | HOH583 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 290 |
| Details | Domain: {"description":"KARI C-terminal knotted","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26876563","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
