2D4V
Crystal structure of NAD dependent isocitrate dehydrogenase from Acidithiobacillus thiooxidans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| C | 0006097 | biological_process | glyoxylate cycle |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
| D | 0006097 | biological_process | glyoxylate cycle |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FLC A 3001 |
| Chain | Residue |
| A | THR105 |
| A | HOH3164 |
| B | LYS230 |
| B | ASN232 |
| B | ASP296 |
| A | SER113 |
| A | ASN115 |
| A | ARG119 |
| A | ARG129 |
| A | ARG153 |
| A | TYR160 |
| A | ASP320 |
| A | NAD2001 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FLC B 3101 |
| Chain | Residue |
| A | LYS230 |
| A | ASN232 |
| A | ILE233 |
| B | THR105 |
| B | SER113 |
| B | ASN115 |
| B | ARG119 |
| B | ARG129 |
| B | ARG153 |
| B | TYR160 |
| B | ASP320 |
| B | NAD2101 |
| B | HOH3150 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FLC C 3201 |
| Chain | Residue |
| C | THR105 |
| C | SER113 |
| C | ASN115 |
| C | ARG119 |
| C | ARG129 |
| C | ARG153 |
| C | TYR160 |
| C | ASP320 |
| C | NAD2201 |
| C | HOH3247 |
| D | LYS230 |
| D | ASN232 |
| D | ILE233 |
| D | ASP296 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FLC D 3301 |
| Chain | Residue |
| C | LYS230 |
| C | ASN232 |
| C | ILE233 |
| C | ASP296 |
| C | HOH3279 |
| D | THR105 |
| D | SER113 |
| D | ASN115 |
| D | ARG119 |
| D | ARG129 |
| D | ARG153 |
| D | TYR160 |
| D | ASP320 |
| D | NAD2301 |
| D | HOH3552 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 2001 |
| Chain | Residue |
| A | ILE37 |
| A | LYS100 |
| A | PRO102 |
| A | LEU103 |
| A | GLU104 |
| A | THR105 |
| A | ASN115 |
| A | ILE333 |
| A | GLU349 |
| A | THR351 |
| A | HIS352 |
| A | GLY353 |
| A | THR354 |
| A | ALA355 |
| A | ASP357 |
| A | ALA364 |
| A | ASN365 |
| A | ASP405 |
| A | FLC3001 |
| A | HOH3016 |
| A | HOH3038 |
| A | HOH3070 |
| A | HOH3108 |
| A | HOH3125 |
| A | HOH3151 |
| A | HOH3171 |
| A | HOH3186 |
| B | ASN232 |
| B | ILE294 |
| B | ASN297 |
| B | GLN300 |
| site_id | AC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 2101 |
| Chain | Residue |
| B | GLU349 |
| B | THR351 |
| B | HIS352 |
| B | GLY353 |
| B | THR354 |
| B | ALA355 |
| B | ASP357 |
| B | ALA364 |
| B | ASN365 |
| B | ASP405 |
| B | FLC3101 |
| B | HOH3130 |
| B | HOH3133 |
| B | HOH3151 |
| B | HOH3165 |
| B | HOH3271 |
| B | HOH3314 |
| A | ASN232 |
| A | ILE294 |
| A | ASN297 |
| A | GLN300 |
| A | HOH3058 |
| A | HOH3060 |
| B | ILE37 |
| B | LYS100 |
| B | PRO102 |
| B | LEU103 |
| B | THR105 |
| B | ASN115 |
| B | ILE333 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD C 2201 |
| Chain | Residue |
| C | ILE37 |
| C | LYS100 |
| C | PRO102 |
| C | LEU103 |
| C | GLU104 |
| C | THR105 |
| C | ASN115 |
| C | ILE333 |
| C | GLU349 |
| C | THR351 |
| C | HIS352 |
| C | GLY353 |
| C | THR354 |
| C | ALA355 |
| C | ASP357 |
| C | ALA364 |
| C | ASN365 |
| C | ASP405 |
| C | FLC3201 |
| C | HOH3210 |
| C | HOH3227 |
| C | HOH3330 |
| C | HOH3336 |
| C | HOH3362 |
| C | HOH3421 |
| D | ASN232 |
| D | ILE294 |
| D | ASN297 |
| D | GLN300 |
| D | HOH3346 |
| D | HOH3407 |
| site_id | AC8 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 2301 |
| Chain | Residue |
| C | ASN232 |
| C | ILE294 |
| C | ASN297 |
| C | GLN300 |
| C | HOH3248 |
| D | ILE37 |
| D | LYS100 |
| D | PRO102 |
| D | LEU103 |
| D | GLU104 |
| D | THR105 |
| D | ASN115 |
| D | ILE333 |
| D | GLU349 |
| D | THR351 |
| D | HIS352 |
| D | GLY353 |
| D | THR354 |
| D | ALA355 |
| D | ASP357 |
| D | ALA364 |
| D | ASN365 |
| D | ASP405 |
| D | FLC3301 |
| D | HOH3307 |
| D | HOH3360 |
| D | HOH3366 |
| D | HOH3442 |
| D | HOH3574 |
| D | HOH3625 |
Functional Information from PROSITE/UniProt
| site_id | PS00470 |
| Number of Residues | 20 |
| Details | IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYvSDalAaev.GGIGM |
| Chain | Residue | Details |
| A | ASN316-MET335 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | ASP296 | |
| A | LYS230 | |
| B | TYR160 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| A | TYR160 | |
| B | ASP296 | |
| B | LYS230 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| D | TYR160 | |
| C | ASP296 | |
| C | LYS230 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a05 |
| Chain | Residue | Details |
| C | TYR160 | |
| D | ASP296 | |
| D | LYS230 |
