3ULK
E. coli Ketol-acid reductoisomerase in complex with NADPH and 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 | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | valine biosynthetic process |
| A | 0015940 | biological_process | pantothenate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008677 | molecular_function | 2-dehydropantoate 2-reductase activity |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | valine biosynthetic process |
| B | 0015940 | biological_process | pantothenate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP A 492 |
| Chain | Residue |
| A | GLY44 |
| A | TYR92 |
| A | LEU105 |
| A | THR106 |
| A | PRO107 |
| A | ASP108 |
| A | GLN110 |
| A | HIS111 |
| A | ASP113 |
| A | VAL114 |
| A | SER131 |
| A | CYS45 |
| A | HIS132 |
| A | PRO154 |
| A | HOH515 |
| A | HOH580 |
| A | HOH597 |
| A | HOH613 |
| A | HOH694 |
| A | HOH716 |
| A | HOH766 |
| A | HOH784 |
| A | GLY46 |
| A | HOH786 |
| A | HOH807 |
| A | HOH812 |
| B | GLU74 |
| A | ALA47 |
| A | GLN48 |
| A | ARG68 |
| A | ALA71 |
| A | ARG76 |
| A | SER78 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 493 |
| Chain | Residue |
| A | ALA2 |
| A | ASN3 |
| A | ASN6 |
| A | HOH752 |
| A | HOH857 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 494 |
| Chain | Residue |
| A | ARG11 |
| A | GLN12 |
| A | HOH559 |
| A | HOH870 |
| B | HOH876 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 495 |
| Chain | Residue |
| A | ARG162 |
| A | LYS166 |
| A | HOH672 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 496 |
| Chain | Residue |
| A | HIS201 |
| A | ARG202 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 497 |
| Chain | Residue |
| A | ARG284 |
| A | LEU288 |
| A | GLN291 |
| A | PHE435 |
| A | GLU438 |
| A | HOH600 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 498 |
| Chain | Residue |
| A | ASP217 |
| A | GLU389 |
| A | GLU393 |
| A | HOH761 |
| A | HOH762 |
| A | HOH763 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 499 |
| Chain | Residue |
| A | ASP217 |
| A | GLU221 |
| A | HOH763 |
| A | HOH764 |
| A | HOH771 |
| A | HOH773 |
| A | HOH775 |
| site_id | AC9 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NDP B 492 |
| Chain | Residue |
| A | GLU74 |
| B | GLY44 |
| B | CYS45 |
| B | GLY46 |
| B | ALA47 |
| B | GLN48 |
| B | ARG68 |
| B | ALA71 |
| B | ARG76 |
| B | SER78 |
| B | TYR92 |
| B | LEU105 |
| B | THR106 |
| B | PRO107 |
| B | ASP108 |
| B | GLN110 |
| B | HIS111 |
| B | ASP113 |
| B | VAL114 |
| B | SER131 |
| B | HIS132 |
| B | PRO154 |
| B | HOH522 |
| B | HOH528 |
| B | HOH530 |
| B | HOH574 |
| B | HOH582 |
| B | HOH749 |
| B | HOH750 |
| B | HOH798 |
| B | HOH813 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 493 |
| Chain | Residue |
| B | ASN3 |
| B | ASN6 |
| B | HOH760 |
| B | HOH785 |
| B | HOH790 |
| B | ALA2 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 494 |
| Chain | Residue |
| A | HOH732 |
| B | ARG11 |
| B | GLN12 |
| B | HOH517 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 495 |
| Chain | Residue |
| B | ARG162 |
| B | LYS166 |
| B | HOH707 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 496 |
| Chain | Residue |
| B | HIS201 |
| B | ARG202 |
| B | HOH590 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 497 |
| Chain | Residue |
| B | ASP217 |
| B | GLU389 |
| B | GLU393 |
| B | HOH765 |
| B | HOH766 |
| B | HOH767 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 498 |
| Chain | Residue |
| B | ASP217 |
| B | HOH766 |
| B | HOH767 |
| B | HOH768 |
| B | HOH774 |
| B | HOH777 |
| B | HOH792 |
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 | HIS132 | |
| B | HIS132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858 |
| Chain | Residue | Details |
| A | ASP108 | |
| A | ASP217 | |
| A | GLU389 | |
| A | GLU393 | |
| B | CYS45 | |
| B | SER78 | |
| B | ASP108 | |
| B | ASP217 | |
| B | GLU389 | |
| B | GLU393 | |
| A | CYS45 | |
| A | SER78 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:9015391 |
| Chain | Residue | Details |
| A | ARG68 | |
| B | ARG68 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000305|PubMed:9015391 |
| Chain | Residue | Details |
| A | ARG76 | |
| B | ARG76 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | SER414 | |
| B | GLY158 | |
| B | GLU221 | |
| B | SER414 | |
| A | GLY158 | |
| A | GLU221 |
