5H92
Crystal structure of the complex between maize Sulfite Reductase and ferredoxin in the form-3 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 | 0009532 | cellular_component | plastid stroma |
| A | 0009570 | cellular_component | chloroplast stroma |
| 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 | 0009532 | cellular_component | plastid stroma |
| B | 0009570 | cellular_component | chloroplast stroma |
| 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 |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue SF4 A 701 |
| Chain | Residue |
| A | CYS494 |
| A | SRM702 |
| A | CYS500 |
| A | ALA503 |
| A | THR538 |
| A | GLY539 |
| A | CYS540 |
| A | ASN542 |
| A | GLY543 |
| A | CYS544 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | binding site for residue SRM A 702 |
| Chain | Residue |
| A | TYR106 |
| A | GLN108 |
| A | ARG124 |
| 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 | LEU502 |
| A | ASN542 |
| A | GLY543 |
| A | CYS544 |
| A | ARG546 |
| A | SF4701 |
| A | PO4703 |
| A | HOH816 |
| A | HOH817 |
| A | HOH849 |
| A | HOH879 |
| A | HOH889 |
| A | HOH899 |
| A | HOH904 |
| A | HOH932 |
| A | HOH969 |
| A | HOH993 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 703 |
| Chain | Residue |
| A | ARG124 |
| A | ARG193 |
| A | LYS276 |
| A | LYS278 |
| A | SRM702 |
| A | HOH804 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 704 |
| Chain | Residue |
| A | VAL424 |
| A | ASN453 |
| A | ASN455 |
| A | HOH825 |
| A | HOH884 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue SF4 B 701 |
| Chain | Residue |
| B | CYS494 |
| B | PRO495 |
| B | CYS500 |
| B | ALA503 |
| B | THR538 |
| B | GLY539 |
| B | CYS540 |
| B | ASN542 |
| B | GLY543 |
| B | CYS544 |
| B | SRM702 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | binding site for residue SRM B 702 |
| Chain | Residue |
| B | CYS544 |
| B | ARG546 |
| B | SF4701 |
| B | PO4703 |
| B | HOH805 |
| B | HOH807 |
| B | HOH811 |
| B | HOH812 |
| B | HOH836 |
| B | HOH849 |
| B | HOH895 |
| B | HOH898 |
| B | HOH909 |
| 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 |
| site_id | AC7 |
| 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 | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 704 |
| Chain | Residue |
| B | VAL424 |
| B | ASN453 |
| B | ASN455 |
| B | HOH832 |
| B | HOH890 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue FES C 101 |
| Chain | Residue |
| C | SER38 |
| C | CYS39 |
| C | ARG40 |
| C | GLY42 |
| C | SER43 |
| C | CYS44 |
| C | CYS47 |
| C | LEU75 |
| C | CYS77 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGSCSSC |
| Chain | Residue | Details |
| C | CYS39-CYS47 |
| 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 | 44 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 90 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
