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 |