5H8V
Crystal structure of the complex between maize Sulfite Reductase and ferredoxin in the form-1 crystal
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003690 | molecular_function | double-stranded DNA binding |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| A | 0009409 | biological_process | response to cold |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0010319 | cellular_component | stromule |
| A | 0016002 | molecular_function | sulfite reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019418 | biological_process | sulfide oxidation |
| A | 0020037 | molecular_function | heme binding |
| A | 0042644 | cellular_component | chloroplast nucleoid |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 1900160 | biological_process | plastid chromosome packaging |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003690 | molecular_function | double-stranded DNA binding |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009337 | cellular_component | sulfite reductase complex (NADPH) |
| B | 0009409 | biological_process | response to cold |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0010319 | cellular_component | stromule |
| B | 0016002 | molecular_function | sulfite reductase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019418 | biological_process | sulfide oxidation |
| B | 0020037 | molecular_function | heme binding |
| B | 0042644 | cellular_component | chloroplast nucleoid |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050311 | molecular_function | sulfite reductase (ferredoxin) activity |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 1900160 | biological_process | plastid chromosome packaging |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 A 701 |
| Chain | Residue |
| A | CYS494 |
| A | CYS500 |
| A | ALA503 |
| A | CYS540 |
| A | ASN542 |
| A | CYS544 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | binding site for residue SRM A 702 |
| Chain | Residue |
| A | ARG153 |
| A | THR155 |
| A | THR156 |
| A | ARG157 |
| A | THR159 |
| A | GLN161 |
| A | HIS163 |
| A | ARG275 |
| A | LYS276 |
| A | LYS278 |
| A | GLY318 |
| A | MET319 |
| A | GLY320 |
| A | ARG368 |
| A | GLN454 |
| A | ALA493 |
| A | CYS494 |
| A | PRO495 |
| A | CYS500 |
| A | PRO501 |
| A | ASN542 |
| A | GLY543 |
| A | CYS544 |
| A | ARG546 |
| A | PO4703 |
| A | HOH804 |
| A | HOH805 |
| A | HOH811 |
| A | HOH814 |
| A | HOH854 |
| A | HOH863 |
| A | HOH894 |
| A | HOH908 |
| A | TYR106 |
| A | GLN108 |
| A | ARG124 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 703 |
| Chain | Residue |
| A | ARG124 |
| A | ARG193 |
| A | LYS276 |
| A | LYS278 |
| A | SRM702 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 704 |
| Chain | Residue |
| A | VAL424 |
| A | ASN453 |
| A | ASN455 |
| A | HOH842 |
| A | HOH878 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 705 |
| Chain | Residue |
| A | TYR106 |
| A | GLY189 |
| A | ARG193 |
| A | HOH903 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 B 701 |
| Chain | Residue |
| B | CYS494 |
| B | CYS500 |
| B | ALA503 |
| B | CYS540 |
| B | ASN542 |
| B | CYS544 |
| site_id | AC7 |
| Number of Residues | 40 |
| Details | binding site for residue SRM B 702 |
| Chain | Residue |
| B | HOH882 |
| B | HOH900 |
| B | HOH925 |
| B | TYR106 |
| B | GLN108 |
| B | ARG124 |
| B | ARG153 |
| B | THR155 |
| B | THR156 |
| B | ARG157 |
| B | THR159 |
| B | GLN161 |
| B | HIS163 |
| B | ARG275 |
| B | LYS276 |
| B | LYS278 |
| B | GLY318 |
| B | MET319 |
| B | GLY320 |
| B | ARG368 |
| B | GLN454 |
| B | ALA493 |
| B | CYS494 |
| B | PRO495 |
| B | LEU499 |
| B | CYS500 |
| B | PRO501 |
| B | LEU502 |
| B | ASN542 |
| B | GLY543 |
| B | CYS544 |
| B | ARG546 |
| B | PO4703 |
| B | HOH835 |
| B | HOH847 |
| B | HOH854 |
| B | HOH856 |
| B | HOH869 |
| B | HOH878 |
| B | HOH881 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 703 |
| Chain | Residue |
| B | ARG124 |
| B | ARG193 |
| B | LYS276 |
| B | LYS278 |
| B | SRM702 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 704 |
| Chain | Residue |
| B | VAL424 |
| B | ASN453 |
| B | ASN455 |
| B | HOH872 |
| B | HOH886 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 705 |
| Chain | Residue |
| B | TYR106 |
| B | GLY189 |
| B | ARG193 |
| B | HOH932 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide TYR B 106 and CYS B 188 |
| Chain | Residue |
| B | LYS101 |
| B | PHE102 |
| B | SER105 |
| B | GLN107 |
| B | GLN108 |
| B | PHE121 |
| B | MET122 |
| B | ARG124 |
| B | GLY186 |
| B | ALA187 |
| B | GLY189 |
| B | ARG193 |
| B | SRM702 |
| B | MG705 |
Functional Information from PROSITE/UniProt
| site_id | PS00365 |
| Number of Residues | 17 |
| Details | NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpngCarpymaELGF |
| Chain | Residue | Details |
| A | THR538-PHE554 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS494 | |
| A | CYS500 | |
| A | CYS540 | |
| B | CYS494 | |
| B | CYS500 | |
| B | CYS540 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS544 | |
| B | CYS544 |
