3TY4
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic process |
| A | 0009085 | biological_process | lysine 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 | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic process |
| B | 0009085 | biological_process | lysine 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 | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047046 | molecular_function | homoisocitrate dehydrogenase activity |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 363 |
| Chain | Residue |
| A | ASP44 |
| A | LEU45 |
| A | ASP46 |
| A | THR63 |
| A | ARG66 |
| A | HOH447 |
| B | ARG27 |
| B | ASN350 |
| B | HOH575 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 364 |
| Chain | Residue |
| A | HIS186 |
| A | LYS188 |
| A | CYS244 |
| A | HOH367 |
| A | HOH466 |
| A | HOH539 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 365 |
| Chain | Residue |
| A | ILE17 |
| A | HIS288 |
| A | ALA300 |
| A | ASN301 |
| A | ASP342 |
| A | HOH505 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 366 |
| Chain | Residue |
| A | ASP260 |
| A | HOH591 |
| B | SER233 |
| B | TYR236 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 363 |
| Chain | Residue |
| B | LYS110 |
| B | ASP121 |
| B | ARG174 |
| B | ILE177 |
| B | ARG178 |
| B | SER184 |
| B | GOL365 |
| B | HOH388 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 364 |
| Chain | Residue |
| B | ILE170 |
| B | SER173 |
| B | GLU314 |
| B | HOH395 |
| B | HOH483 |
| B | HOH595 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 365 |
| Chain | Residue |
| B | PRO108 |
| B | ARG174 |
| B | GLU314 |
| B | GOL363 |
| B | HOH383 |
| B | HOH385 |
| B | HOH388 |
| B | HOH395 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 366 |
| Chain | Residue |
| B | ARG26 |
| B | PHE42 |
| B | ASP44 |
| B | HOH407 |
| B | HOH414 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 367 |
| Chain | Residue |
| B | HIS186 |
| B | LYS188 |
| B | LEU190 |
| B | CYS244 |
| B | HOH539 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 368 |
| Chain | Residue |
| A | SER233 |
| A | TYR236 |
| B | ARG107 |
| B | ASP260 |
| B | HOH647 |
| B | HOH661 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDgaAsli.GSLGL |
| Chain | Residue | Details |
| A | ASN252-LEU271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q72IW9 |
| Chain | Residue | Details |
| A | VAL79 | |
| B | LYS196 | |
| B | ASN198 | |
| B | ASP232 | |
| B | ASP256 | |
| B | ASP260 | |
| B | GLY289 | |
| B | ASN301 | |
| A | LYS196 | |
| A | ASN198 | |
| A | ASP232 | |
| A | ASP256 | |
| A | ASP260 | |
| A | GLY289 | |
| A | ASN301 | |
| B | VAL79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: in other chain => ECO:0000250|UniProtKB:Q72IW9 |
| Chain | Residue | Details |
| A | SER81 | |
| B | TYR133 | |
| A | ARG97 | |
| A | ARG107 | |
| A | ARG126 | |
| A | TYR133 | |
| B | SER81 | |
| B | ARG97 | |
| B | ARG107 | |
| B | ARG126 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18257517 |
| Chain | Residue | Details |
| A | SER81 | |
| A | SER91 | |
| B | SER81 | |
| B | SER91 |
