6IXL
Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
A | 0006102 | biological_process | isocitrate metabolic process |
B | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
B | 0006102 | biological_process | isocitrate metabolic process |
C | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
C | 0006102 | biological_process | isocitrate metabolic process |
D | 0004450 | molecular_function | isocitrate dehydrogenase (NADP+) activity |
D | 0006102 | biological_process | isocitrate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | HIS339 |
A | GLY340 |
A | THR341 |
A | VAL342 |
A | HOH607 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | ASP302 |
A | SO4503 |
A | HOH749 |
B | LYS234 |
A | ASN118 |
A | ARG122 |
A | ARG152 |
A | TYR159 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | THR99 |
A | SER116 |
A | ASN118 |
A | SO4502 |
A | HOH749 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | HIS339 |
B | GLY340 |
B | THR341 |
B | VAL342 |
B | HOH602 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL B 502 |
Chain | Residue |
B | ASN378 |
B | ILE379 |
B | ASP380 |
B | ARG381 |
B | ASP382 |
B | HOH623 |
B | HOH727 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
B | ASN118 |
B | ARG122 |
B | ARG152 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
C | ASN378 |
C | ILE379 |
C | ASP380 |
C | ARG381 |
C | ASP382 |
C | HOH608 |
C | HOH661 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | THR228 |
C | TYR230 |
C | TRP287 |
C | GLN289 |
C | PHE292 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 503 |
Chain | Residue |
C | GLY119 |
C | ARG123 |
C | HOH640 |
C | HOH773 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue GOL D 501 |
Chain | Residue |
D | GLY340 |
D | THR341 |
D | VAL342 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
D | ASN118 |
D | ARG122 |
D | ARG152 |
D | TYR159 |
D | HOH601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXN |
Chain | Residue | Details |
A | THR97 | |
C | ASN118 | |
C | LYS283 | |
C | HIS339 | |
D | THR97 | |
D | ASN118 | |
D | LYS283 | |
D | HIS339 | |
A | ASN118 | |
A | LYS283 | |
A | HIS339 | |
B | THR97 | |
B | ASN118 | |
B | LYS283 | |
B | HIS339 | |
C | THR97 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:7E2W |
Chain | Residue | Details |
A | SER116 | |
C | ARG152 | |
C | TYR159 | |
C | LYS234 | |
D | SER116 | |
D | ARG152 | |
D | TYR159 | |
D | LYS234 | |
A | ARG152 | |
A | TYR159 | |
A | LYS234 | |
B | SER116 | |
B | ARG152 | |
B | TYR159 | |
B | LYS234 | |
C | SER116 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXT |
Chain | Residue | Details |
A | ASP278 | |
D | ASP278 | |
D | ASP302 | |
D | ASP306 | |
A | ASP302 | |
A | ASP306 | |
B | ASP278 | |
B | ASP302 | |
B | ASP306 | |
C | ASP278 | |
C | ASP302 | |
C | ASP306 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:6IXN, ECO:0007744|PDB:6IXT |
Chain | Residue | Details |
A | ASN358 | |
B | ASN358 | |
C | ASN358 | |
D | ASN358 |