2D1C
Crystal Structure Of TT0538 protein from Thermus thermophilus HB8
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 | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006102 | biological_process | isocitrate metabolic 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 | 0046872 | molecular_function | metal ion binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004449 | molecular_function | isocitrate dehydrogenase (NAD+) activity |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006102 | biological_process | isocitrate metabolic 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 1002 |
| Chain | Residue |
| A | LYS85 |
| A | HIS280 |
| A | GLY281 |
| A | SER282 |
| A | ALA283 |
| A | LYS285 |
| A | TYR286 |
| A | ILE292 |
| A | ASN293 |
| A | ASP334 |
| A | CIT1585 |
| A | PRO87 |
| A | HOH1618 |
| A | HOH1717 |
| A | HOH1800 |
| A | HOH1810 |
| A | HOH1839 |
| A | HOH1975 |
| B | ASN193 |
| B | ILE222 |
| B | ASN225 |
| B | HIS228 |
| A | LEU88 |
| B | GLN229 |
| B | LYS232 |
| B | HOH1669 |
| B | HOH1975 |
| A | GLU89 |
| A | THR90 |
| A | ASN100 |
| A | LEU261 |
| A | GLU277 |
| A | VAL279 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAP B 1003 |
| Chain | Residue |
| A | ASN193 |
| A | ILE222 |
| A | ASN225 |
| A | GLN229 |
| A | LYS232 |
| A | HOH1625 |
| A | HOH1759 |
| B | LYS85 |
| B | PRO87 |
| B | LEU88 |
| B | GLU89 |
| B | THR90 |
| B | ASN100 |
| B | LEU261 |
| B | GLU277 |
| B | VAL279 |
| B | HIS280 |
| B | GLY281 |
| B | SER282 |
| B | ALA283 |
| B | LYS285 |
| B | TYR286 |
| B | ILE292 |
| B | ASN293 |
| B | ASP334 |
| B | CIT1586 |
| B | HOH1612 |
| B | HOH1687 |
| B | HOH1711 |
| B | HOH1745 |
| B | HOH1816 |
| B | HOH1840 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT A 1585 |
| Chain | Residue |
| A | THR90 |
| A | SER98 |
| A | ASN100 |
| A | ARG104 |
| A | ARG114 |
| A | ARG137 |
| A | TYR144 |
| A | ASP248 |
| A | NAP1002 |
| B | LYS191 |
| B | ASN193 |
| B | ASP224 |
| B | HOH1693 |
| B | HOH1854 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT B 1586 |
| Chain | Residue |
| A | LYS191 |
| A | ASN193 |
| A | ASP224 |
| B | THR90 |
| B | SER98 |
| B | ASN100 |
| B | ARG104 |
| B | ARG114 |
| B | ARG137 |
| B | TYR144 |
| B | ASP248 |
| B | NAP1003 |
| B | HOH1688 |
| B | HOH1698 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NMNGDIlSDltSgli.GGLGF |
| Chain | Residue | Details |
| A | ASN244-PHE263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG104 | |
| B | ASP224 | |
| B | ASP248 | |
| B | ASP252 | |
| A | ARG114 | |
| A | ARG137 | |
| A | ASP224 | |
| A | ASP248 | |
| A | ASP252 | |
| B | ARG104 | |
| B | ARG114 | |
| B | ARG137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Critical for catalysis => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR144 | |
| A | LYS191 | |
| B | TYR144 | |
| B | LYS191 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250 |
| Chain | Residue | Details |
| A | SER98 | |
| B | SER98 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP224 | |
| A | LYS191 | |
| B | TYR144 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR144 | |
| B | ASP224 | |
| B | LYS191 |
