Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0004783 | molecular_function | sulfite reductase (NADPH) activity | 
| A | 0008652 | biological_process | amino acid biosynthetic process | 
| A | 0009337 | cellular_component | sulfite reductase complex (NADPH) | 
| A | 0016491 | molecular_function | oxidoreductase activity | 
| A | 0020037 | molecular_function | heme binding | 
| A | 0050661 | molecular_function | NADP binding | 
| A | 0051536 | molecular_function | iron-sulfur cluster binding | 
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE PO4 A 585 | 
| Chain | Residue | 
| A | LYS217 | 
| A | SRM580 | 
| A | HOH709 | 
| A | ARG83 | 
| A | ARG117 | 
| A | ARG153 | 
| A | LYS215 | 
| site_id | AC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE K A 590 | 
| Chain | Residue | 
| A | ILE362 | 
| A | ASN395 | 
| A | GLN396 | 
| A | ASN397 | 
| A | HOH640 | 
| A | HOH642 | 
| site_id | AC3 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE SF4 A 575 | 
| Chain | Residue | 
| A | CYS434 | 
| A | CYS440 | 
| A | ALA443 | 
| A | THR477 | 
| A | CYS479 | 
| A | ASN481 | 
| A | CYS483 | 
| A | SRM580 | 
| site_id | AC4 | 
| Number of Residues | 41 | 
| Details | BINDING SITE FOR RESIDUE SRM A 580 | 
| Chain | Residue | 
| A | ARG83 | 
| A | ARG113 | 
| A | THR115 | 
| A | ASN116 | 
| A | ARG117 | 
| A | THR119 | 
| A | GLN121 | 
| A | HIS123 | 
| A | ARG214 | 
| A | LYS215 | 
| A | LYS217 | 
| A | GLY256 | 
| A | LEU257 | 
| A | SER258 | 
| A | GLN396 | 
| A | ALA433 | 
| A | CYS434 | 
| A | VAL435 | 
| A | THR439 | 
| A | CYS440 | 
| A | PRO441 | 
| A | ASN481 | 
| A | GLY482 | 
| A | CYS483 | 
| A | ARG485 | 
| A | SF4575 | 
| A | PO4585 | 
| A | HOH607 | 
| A | HOH694 | 
| A | HOH695 | 
| A | HOH717 | 
| A | HOH743 | 
| A | HOH771 | 
| A | HOH772 | 
| A | HOH773 | 
| A | HOH774 | 
| A | HOH827 | 
| A | HOH832 | 
| A | HOH887 | 
| A | HOH901 | 
| A | HOH966 | 
| site_id | ACT | 
| Number of Residues | 4 | 
| Details | FOUR ACTIVE SITE RESIDUES THAT CONTACT THE BOUND PHOSPHATE. | 
| Chain | Residue | 
| A | ARG83 | 
| A | ARG153 | 
| A | LYS215 | 
| A | LYS217 | 
| site_id | BRG | 
| Number of Residues | 1 | 
| Details | CYSTEINE THIOLATE IN THE ACTIVE CENTER THAT BRIDGES THE HEME IRON TO THE [4FE-4S] CLUSTER. | 
Functional Information from PROSITE/UniProt
| site_id | PS00365 | 
| Number of Residues | 17 | 
| Details | NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpngCgramlaEVGL | 
| Chain | Residue | Details | 
| A | THR477-LEU493 |  | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 3 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7569952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9315848","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 1 | 
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7569952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9315848","evidenceCode":"ECO:0000269"}]} | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 5 | 
| Details | a catalytic site defined by CSA, PubMed 9315848, 7569952, 10984484, 9315849, 15966732 | 
| Chain | Residue | Details | 
| A | LYS215 |  | 
| A | ARG83 |  | 
| A | CYS483 |  | 
| A | LYS217 |  | 
| A | ARG153 |  | 
| site_id | MCSA1 | 
| Number of Residues | 8 | 
| Details | M-CSA 398 | 
| Chain | Residue | Details | 
| A | ARG83 | activator | 
| A | ARG153 | activator | 
| A | LYS215 | activator | 
| A | LYS217 | activator | 
| A | CYS434 | metal ligand | 
| A | CYS440 | metal ligand | 
| A | CYS479 | metal ligand | 
| A | CYS483 | electron shuttle, metal ligand |