4XDY
Structure of NADH-preferring ketol-acid reductoisomerase from an uncultured archean
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 | 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 | 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 | ASP195 |
| A | GLU199 |
| A | MG402 |
| A | HIO406 |
| A | HOH528 |
| A | HOH647 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH527 |
| B | HOH539 |
| B | HOH540 |
| A | ASP195 |
| A | MG401 |
| A | HIO406 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | binding site for residue NAI A 403 |
| Chain | Residue |
| A | GLY25 |
| A | ALA26 |
| A | GLN27 |
| A | GLU46 |
| A | LEU50 |
| A | ASN55 |
| A | SER57 |
| A | LEU84 |
| A | LEU85 |
| A | PRO86 |
| A | ASP87 |
| A | VAL89 |
| A | GLN90 |
| A | ILE93 |
| A | SER111 |
| A | HIS112 |
| A | PRO134 |
| A | ALA136 |
| A | PRO137 |
| A | GLY138 |
| A | HIO406 |
| A | HOH531 |
| A | HOH539 |
| A | HOH541 |
| A | HOH544 |
| A | HOH590 |
| A | HOH625 |
| A | HOH633 |
| A | HOH647 |
| A | HOH648 |
| A | HOH663 |
| B | VAL254 |
| B | ILE255 |
| B | SER256 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | ASN257 |
| A | HOH533 |
| A | HOH623 |
| A | HOH630 |
| A | HOH665 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ASP29 |
| A | ASN33 |
| A | LYS60 |
| A | ASP64 |
| A | ARG142 |
| A | HOH575 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | binding site for residue HIO A 406 |
| Chain | Residue |
| A | PRO137 |
| A | ASP195 |
| A | GLU199 |
| A | CYS204 |
| A | MG401 |
| A | MG402 |
| A | NAI403 |
| A | HOH527 |
| A | HOH528 |
| A | HOH647 |
| B | GLU235 |
| B | ILE239 |
| B | ILE255 |
| B | SER256 |
| B | ALA259 |
| B | HOH539 |
| B | HOH540 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue HIO B 401 |
| Chain | Residue |
| A | GLU235 |
| A | ILE239 |
| A | ILE255 |
| A | SER256 |
| A | ALA259 |
| A | HOH525 |
| A | HOH526 |
| B | PRO137 |
| B | ASP195 |
| B | GLU199 |
| B | CYS204 |
| B | MG402 |
| B | MG403 |
| B | NAI404 |
| B | HOH536 |
| B | HOH537 |
| B | HOH538 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP195 |
| B | GLU199 |
| B | HIO401 |
| B | MG403 |
| B | HOH536 |
| B | HOH537 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASP195 |
| B | HIO401 |
| B | MG402 |
| B | HOH538 |
| A | HOH525 |
| A | HOH526 |
| site_id | AD1 |
| Number of Residues | 36 |
| Details | binding site for residue NAI B 404 |
| Chain | Residue |
| A | VAL254 |
| A | ILE255 |
| A | SER256 |
| A | HOH623 |
| B | GLY25 |
| B | ALA26 |
| B | GLN27 |
| B | GLU46 |
| B | LEU50 |
| B | ASN55 |
| B | SER57 |
| B | LEU84 |
| B | LEU85 |
| B | PRO86 |
| B | ASP87 |
| B | VAL89 |
| B | GLN90 |
| B | ILE93 |
| B | SER111 |
| B | HIS112 |
| B | PRO134 |
| B | ALA136 |
| B | PRO137 |
| B | GLY138 |
| B | HIO401 |
| B | HOH512 |
| B | HOH525 |
| B | HOH537 |
| B | HOH545 |
| B | HOH553 |
| B | HOH557 |
| B | HOH562 |
| B | HOH571 |
| B | HOH575 |
| B | HOH640 |
| B | HOH682 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 405 |
| Chain | Residue |
| A | HOH625 |
| B | ASN257 |
| B | HOH551 |
| B | HOH649 |
| B | HOH694 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | ASP29 |
| B | ASN33 |
| B | LYS60 |
| B | ASP64 |
| B | ARG142 |
| B | HOH599 |
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 | HIS112 | |
| B | HIS112 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:25849365 |
| Chain | Residue | Details |
| A | TYR24 | |
| B | ASN55 | |
| B | SER57 | |
| B | ASP87 | |
| B | GLY138 | |
| B | GLU199 | |
| A | GLU46 | |
| A | ASN55 | |
| A | SER57 | |
| A | ASP87 | |
| A | GLY138 | |
| A | GLU199 | |
| B | TYR24 | |
| B | GLU46 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435 |
| Chain | Residue | Details |
| A | ASP195 | |
| A | GLU231 | |
| A | GLU235 | |
| A | SER256 | |
| B | ASP195 | |
| B | GLU231 | |
| B | GLU235 | |
| B | SER256 |
