6IXN
Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri in complex with NAD+ and citrate
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 | 8 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ARG381 |
| A | ASP382 |
| A | HOH635 |
| A | HOH639 |
| A | HOH642 |
| A | HOH717 |
| C | HOH615 |
| C | HOH648 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | ARG400 |
| A | HOH603 |
| A | HOH628 |
| A | HIS396 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TYR230 |
| A | TRP287 |
| A | GLN289 |
| A | HOH646 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue FLC A 504 |
| Chain | Residue |
| A | THR99 |
| A | SER116 |
| A | ASN118 |
| A | ARG122 |
| A | ARG132 |
| A | ARG152 |
| A | TYR159 |
| A | ASP302 |
| A | NAD505 |
| A | HOH699 |
| A | HOH738 |
| A | HOH747 |
| B | LYS234 |
| B | VAL237 |
| B | ASP278 |
| B | HOH757 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | binding site for residue NAD A 505 |
| Chain | Residue |
| A | LYS94 |
| A | PRO96 |
| A | THR97 |
| A | VAL98 |
| A | THR99 |
| A | ASN118 |
| A | HIS339 |
| A | GLY340 |
| A | THR341 |
| A | VAL342 |
| A | ASP344 |
| A | MET345 |
| A | ASN358 |
| A | FLC504 |
| A | HOH612 |
| A | HOH622 |
| A | HOH630 |
| A | HOH636 |
| A | HOH650 |
| A | HOH690 |
| A | HOH695 |
| A | HOH714 |
| A | HOH722 |
| A | HOH743 |
| A | HOH759 |
| A | HOH769 |
| B | LEU276 |
| B | ALA279 |
| B | MET282 |
| B | LYS283 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | ARG381 |
| B | ASP382 |
| B | HOH651 |
| B | HOH678 |
| B | HOH697 |
| B | HOH720 |
| D | HOH604 |
| D | HOH611 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | THR393 |
| B | HIS396 |
| B | ARG400 |
| B | HOH607 |
| B | HOH661 |
| B | HOH721 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | THR228 |
| B | TYR230 |
| B | GLN289 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue PEG B 504 |
| Chain | Residue |
| B | ARG123 |
| B | VAL155 |
| B | GLY156 |
| B | TYR159 |
| B | SER160 |
| B | HOH606 |
| B | HOH656 |
| B | HOH727 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue FLC B 505 |
| Chain | Residue |
| B | HOH657 |
| B | HOH706 |
| B | HOH736 |
| A | LYS234 |
| A | VAL237 |
| A | ASP278 |
| B | THR99 |
| B | SER116 |
| B | ASN118 |
| B | ARG122 |
| B | ARG132 |
| B | ARG152 |
| B | TYR159 |
| B | ASP302 |
| B | NAD506 |
| site_id | AD2 |
| Number of Residues | 30 |
| Details | binding site for residue NAD B 506 |
| Chain | Residue |
| A | LEU276 |
| A | ALA279 |
| A | MET282 |
| A | LYS283 |
| A | HOH700 |
| B | LYS94 |
| B | PRO96 |
| B | THR97 |
| B | THR99 |
| B | ASN118 |
| B | HIS339 |
| B | GLY340 |
| B | THR341 |
| B | VAL342 |
| B | ASP344 |
| B | MET345 |
| B | ASN358 |
| B | FLC505 |
| B | HOH610 |
| B | HOH614 |
| B | HOH633 |
| B | HOH635 |
| B | HOH679 |
| B | HOH707 |
| B | HOH734 |
| B | HOH740 |
| B | HOH752 |
| B | HOH760 |
| B | HOH775 |
| B | HOH780 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 C 501 |
| Chain | Residue |
| A | HOH614 |
| A | HOH634 |
| C | ARG381 |
| C | ASP382 |
| C | HOH679 |
| C | HOH680 |
| C | HOH718 |
| C | HOH764 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| C | THR393 |
| C | HIS396 |
| C | ARG400 |
| C | HOH696 |
| C | HOH820 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | THR228 |
| C | TYR230 |
| C | TRP287 |
| C | GLN289 |
| C | HOH602 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue FLC C 504 |
| Chain | Residue |
| C | THR99 |
| C | SER116 |
| C | ASN118 |
| C | ARG122 |
| C | ARG132 |
| C | ARG152 |
| C | TYR159 |
| C | ASP302 |
| C | NAD505 |
| C | HOH635 |
| C | HOH758 |
| D | LYS234 |
| D | VAL237 |
| D | ASP278 |
| D | HOH636 |
| site_id | AD7 |
| Number of Residues | 30 |
| Details | binding site for residue NAD C 505 |
| Chain | Residue |
| C | LYS94 |
| C | PRO96 |
| C | THR97 |
| C | THR99 |
| C | ASN118 |
| C | PRO315 |
| C | HIS339 |
| C | GLY340 |
| C | THR341 |
| C | VAL342 |
| C | ASP344 |
| C | MET345 |
| C | ASN358 |
| C | FLC504 |
| C | HOH611 |
| C | HOH619 |
| C | HOH625 |
| C | HOH653 |
| C | HOH668 |
| C | HOH673 |
| C | HOH687 |
| C | HOH689 |
| C | HOH731 |
| C | HOH747 |
| C | HOH755 |
| C | HOH786 |
| D | LEU276 |
| D | ALA279 |
| D | MET282 |
| D | LYS283 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 D 501 |
| Chain | Residue |
| B | HOH668 |
| D | ASP380 |
| D | ARG381 |
| D | ASP382 |
| D | HOH606 |
| D | HOH614 |
| D | HOH620 |
| D | HOH720 |
| D | HOH734 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | HIS396 |
| D | ARG400 |
| D | HOH610 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | ARG288 |
| D | GLN310 |
| D | VAL311 |
| D | LYS313 |
| D | HOH630 |
| D | HOH645 |
| D | HOH792 |
| D | HOH797 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | TYR230 |
| D | TRP287 |
| D | GLN289 |
| site_id | AE3 |
| Number of Residues | 14 |
| Details | binding site for residue FLC D 505 |
| Chain | Residue |
| C | LYS234 |
| C | VAL237 |
| C | ASP278 |
| C | HOH629 |
| D | THR99 |
| D | SER116 |
| D | ASN118 |
| D | ARG122 |
| D | ARG132 |
| D | ARG152 |
| D | TYR159 |
| D | ASP302 |
| D | NAD506 |
| D | HOH765 |
| site_id | AE4 |
| Number of Residues | 30 |
| Details | binding site for residue NAD D 506 |
| Chain | Residue |
| C | LEU276 |
| C | ALA279 |
| C | LYS283 |
| C | HOH698 |
| D | LYS94 |
| D | PRO96 |
| D | THR97 |
| D | THR99 |
| D | ASN118 |
| D | PRO315 |
| D | HIS339 |
| D | GLY340 |
| D | THR341 |
| D | VAL342 |
| D | ASP344 |
| D | MET345 |
| D | ASN358 |
| D | FLC505 |
| D | HOH608 |
| D | HOH618 |
| D | HOH628 |
| D | HOH647 |
| D | HOH661 |
| D | HOH674 |
| D | HOH684 |
| D | HOH714 |
| D | HOH723 |
| D | HOH725 |
| D | HOH727 |
| D | HOH837 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"7E2W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of isocitrate dehydrogenase from Ostreococcus tauri.","authors":["Zhu G.P.","Tang W.G.","Wang P."]}},{"source":"PDB","id":"6IXN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IXT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
