3JQQ
Crystal structure of the H286K mutant of Ferredoxin-NADP+ reductase from Plasmodium falciparum in complex with 2'P-AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 415 |
| Chain | Residue |
| A | ARG101 |
| A | GLY136 |
| A | TYR137 |
| A | CYS138 |
| A | SER139 |
| A | THR180 |
| A | TYR316 |
| A | HOH320 |
| A | HOH325 |
| A | HOH335 |
| A | HOH365 |
| A | LEU102 |
| A | HOH383 |
| A | HOH470 |
| B | LEU102 |
| B | HOH410 |
| B | FAD415 |
| A | TYR103 |
| A | SER104 |
| A | ALA117 |
| A | ILE118 |
| A | LYS119 |
| A | HIS121 |
| A | TYR123 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE A2P A 416 |
| Chain | Residue |
| A | LYS119 |
| A | THR178 |
| A | GLY216 |
| A | VAL217 |
| A | TYR218 |
| A | SER247 |
| A | TYR258 |
| A | GLN260 |
| A | LYS286 |
| A | SER288 |
| A | HOH318 |
| A | HOH386 |
| A | HOH442 |
| A | HOH570 |
| A | HOH670 |
| A | HOH673 |
| A | HOH1118 |
| B | TYR258 |
| B | LYS287 |
| B | SER288 |
| B | A2P416 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD B 415 |
| Chain | Residue |
| A | LEU102 |
| A | LYS287 |
| A | HOH376 |
| A | FAD415 |
| B | ARG101 |
| B | LEU102 |
| B | TYR103 |
| B | SER104 |
| B | ALA117 |
| B | ILE118 |
| B | LYS119 |
| B | HIS121 |
| B | TYR123 |
| B | GLY136 |
| B | TYR137 |
| B | CYS138 |
| B | SER139 |
| B | THR180 |
| B | TYR316 |
| B | HOH342 |
| B | HOH372 |
| B | HOH556 |
| B | HOH557 |
| B | HOH569 |
| B | HOH690 |
| B | HOH1085 |
| B | HOH1152 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE A2P B 416 |
| Chain | Residue |
| A | TYR258 |
| A | SER288 |
| A | A2P416 |
| B | LYS119 |
| B | THR178 |
| B | GLY179 |
| B | GLY216 |
| B | VAL217 |
| B | TYR218 |
| B | SER247 |
| B | TYR258 |
| B | GLN260 |
| B | LYS286 |
| B | SER288 |
| B | HOH322 |
| B | HOH330 |
| B | HOH337 |
| B | HOH354 |
| B | HOH430 |
| B | HOH508 |
| B | HOH710 |
| B | HOH1214 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD C 415 |
| Chain | Residue |
| C | ILE118 |
| C | LYS119 |
| C | HIS121 |
| C | TYR123 |
| C | GLY136 |
| C | TYR137 |
| C | CYS138 |
| C | SER139 |
| C | THR180 |
| C | TYR316 |
| C | HOH321 |
| C | HOH329 |
| C | HOH332 |
| C | HOH362 |
| C | HOH368 |
| C | HOH392 |
| C | HOH553 |
| C | HOH706 |
| D | LEU102 |
| D | FAD415 |
| C | ARG101 |
| C | LEU102 |
| C | TYR103 |
| C | SER104 |
| C | ALA117 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE A2P C 416 |
| Chain | Residue |
| C | LYS119 |
| C | GLY216 |
| C | VAL217 |
| C | TYR218 |
| C | SER247 |
| C | TYR258 |
| C | GLN260 |
| C | LYS286 |
| C | SER288 |
| C | HOH325 |
| C | HOH330 |
| C | HOH367 |
| C | HOH393 |
| C | HOH395 |
| C | HOH478 |
| C | HOH562 |
| C | HOH1250 |
| D | TYR258 |
| D | SER288 |
| D | A2P416 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD D 415 |
| Chain | Residue |
| C | LEU102 |
| C | HOH411 |
| C | FAD415 |
| D | ARG101 |
| D | LEU102 |
| D | TYR103 |
| D | SER104 |
| D | ALA117 |
| D | ILE118 |
| D | LYS119 |
| D | HIS121 |
| D | TYR123 |
| D | GLY136 |
| D | TYR137 |
| D | CYS138 |
| D | SER139 |
| D | THR180 |
| D | TYR316 |
| D | HOH317 |
| D | HOH321 |
| D | HOH342 |
| D | HOH357 |
| D | HOH406 |
| D | HOH661 |
| D | HOH820 |
| D | HOH1076 |
| D | HOH1342 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE A2P D 416 |
| Chain | Residue |
| C | TYR258 |
| C | LYS287 |
| C | SER288 |
| C | A2P416 |
| D | LYS119 |
| D | THR178 |
| D | GLY179 |
| D | GLY216 |
| D | VAL217 |
| D | TYR218 |
| D | SER247 |
| D | TYR258 |
| D | GLN260 |
| D | LYS286 |
| D | HOH318 |
| D | HOH330 |
| D | HOH335 |
| D | HOH362 |
| D | HOH591 |
| D | HOH666 |
| D | HOH683 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FAD E 415 |
| Chain | Residue |
| E | ARG101 |
| E | LEU102 |
| E | TYR103 |
| E | SER104 |
| E | ALA117 |
| E | ILE118 |
| E | LYS119 |
| E | HIS121 |
| E | TYR123 |
| E | GLY136 |
| E | TYR137 |
| E | CYS138 |
| E | SER139 |
| E | THR180 |
| E | TYR316 |
| E | HOH317 |
| E | HOH337 |
| E | HOH524 |
| E | HOH699 |
| F | LEU102 |
| F | FAD415 |
| F | HOH588 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A2P E 416 |
| Chain | Residue |
| E | LYS119 |
| E | GLY216 |
| E | VAL217 |
| E | TYR218 |
| E | SER247 |
| E | TYR258 |
| E | GLN260 |
| E | LYS286 |
| E | SER288 |
| E | HOH332 |
| E | HOH509 |
| E | HOH956 |
| F | TYR258 |
| F | LYS287 |
| F | SER288 |
| F | A2P416 |
| site_id | BC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD F 415 |
| Chain | Residue |
| E | LEU102 |
| E | FAD415 |
| E | HOH431 |
| F | ARG101 |
| F | LEU102 |
| F | TYR103 |
| F | SER104 |
| F | ALA117 |
| F | ILE118 |
| F | LYS119 |
| F | HIS121 |
| F | TYR123 |
| F | GLY136 |
| F | TYR137 |
| F | CYS138 |
| F | SER139 |
| F | THR180 |
| F | TYR316 |
| F | HOH325 |
| F | HOH461 |
| F | HOH560 |
| F | HOH689 |
| F | HOH746 |
| F | HOH916 |
| site_id | BC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE A2P F 416 |
| Chain | Residue |
| E | TYR258 |
| E | SER288 |
| E | A2P416 |
| F | LYS119 |
| F | THR178 |
| F | GLY179 |
| F | GLY216 |
| F | VAL217 |
| F | TYR218 |
| F | SER247 |
| F | TYR258 |
| F | LYS286 |
| F | SER288 |
| F | ILE289 |
| F | HOH320 |
| F | HOH332 |
| F | HOH567 |
| F | HOH600 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17258767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OK8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 77 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17258767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19736991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17258767","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19736991","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19736991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JQP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17258767","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19736991","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JQP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19736991","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3JQQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
