4KQW
The structure of the Slackia exigua KARI in complex with NADP
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 | 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 | 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 | 36 |
| Details | BINDING SITE FOR RESIDUE NAP A 401 |
| Chain | Residue |
| A | TYR35 |
| A | PRO92 |
| A | ASP93 |
| A | ILE95 |
| A | GLN96 |
| A | ALA117 |
| A | HIS118 |
| A | PRO140 |
| A | GLY142 |
| A | PRO143 |
| A | GLY144 |
| A | GLY36 |
| A | HOH501 |
| A | HOH507 |
| A | HOH522 |
| A | HOH531 |
| A | HOH563 |
| A | HOH568 |
| A | HOH660 |
| A | HOH664 |
| A | HOH708 |
| A | HOH736 |
| A | SER37 |
| A | HOH746 |
| A | HOH797 |
| B | SER260 |
| B | ILE261 |
| B | SER262 |
| B | TLA401 |
| B | HOH551 |
| A | GLN38 |
| A | ARG58 |
| A | SER61 |
| A | SER63 |
| A | LEU90 |
| A | VAL91 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE TLA A 402 |
| Chain | Residue |
| A | GLU241 |
| A | ILE261 |
| A | SER262 |
| A | ALA265 |
| A | HOH551 |
| A | HOH713 |
| B | GLY142 |
| B | PRO143 |
| B | ASP201 |
| B | GLU205 |
| B | LEU209 |
| B | CYS210 |
| B | NAP402 |
| B | MG404 |
| B | MG405 |
| B | HOH504 |
| B | HOH529 |
| B | HOH604 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TLA A 403 |
| Chain | Residue |
| A | HIS40 |
| A | HIS145 |
| A | ARG148 |
| A | ARG149 |
| A | HOH570 |
| A | HOH774 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 404 |
| Chain | Residue |
| A | ASP201 |
| A | GLU205 |
| A | MG405 |
| A | HOH506 |
| B | TLA401 |
| B | HOH518 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 405 |
| Chain | Residue |
| A | ASP201 |
| A | MG404 |
| A | HOH537 |
| B | TLA401 |
| B | HOH559 |
| B | HOH637 |
| B | HOH951 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE TLA B 401 |
| Chain | Residue |
| A | PRO143 |
| A | ASP201 |
| A | GLU205 |
| A | LEU209 |
| A | CYS210 |
| A | NAP401 |
| A | MG404 |
| A | MG405 |
| A | HOH506 |
| A | HOH537 |
| B | GLU241 |
| B | ILE261 |
| B | SER262 |
| B | ALA265 |
| B | HOH518 |
| B | HOH559 |
| B | HOH951 |
| site_id | AC7 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE NAP B 402 |
| Chain | Residue |
| B | LEU57 |
| B | ARG58 |
| B | SER61 |
| B | SER63 |
| B | LEU90 |
| B | VAL91 |
| B | PRO92 |
| B | ASP93 |
| B | ILE95 |
| B | GLN96 |
| B | ALA117 |
| B | HIS118 |
| B | PRO140 |
| B | GLY142 |
| B | PRO143 |
| B | GLY144 |
| B | HOH502 |
| B | HOH508 |
| B | HOH516 |
| B | HOH563 |
| B | HOH564 |
| B | HOH607 |
| B | HOH617 |
| B | HOH682 |
| B | HOH698 |
| B | HOH733 |
| B | HOH742 |
| B | HOH771 |
| B | HOH803 |
| B | HOH823 |
| A | SER260 |
| A | ILE261 |
| A | SER262 |
| A | TLA402 |
| A | HOH542 |
| B | TYR35 |
| B | GLY36 |
| B | SER37 |
| B | GLN38 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TLA B 403 |
| Chain | Residue |
| B | HIS40 |
| B | HIS145 |
| B | ARG148 |
| B | ARG149 |
| B | HOH952 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| A | TLA402 |
| B | ASP201 |
| B | GLU205 |
| B | MG405 |
| B | HOH504 |
| B | HOH529 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 405 |
| Chain | Residue |
| A | TLA402 |
| A | HOH551 |
| A | HOH554 |
| A | HOH713 |
| B | ASP201 |
| B | MG404 |
| B | HOH604 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | HIS118 | |
| B | HIS118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23776225 |
| Chain | Residue | Details |
| A | TYR35 | |
| B | ARG58 | |
| B | SER61 | |
| B | SER63 | |
| B | ASP93 | |
| B | GLY144 | |
| B | GLU205 | |
| B | SER262 | |
| A | ARG58 | |
| A | SER61 | |
| A | SER63 | |
| A | ASP93 | |
| A | GLY144 | |
| A | GLU205 | |
| A | SER262 | |
| B | TYR35 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | ASP201 | |
| A | GLU237 | |
| A | GLU241 | |
| B | ASP201 | |
| B | GLU237 | |
| B | GLU241 |
