2AKJ
Structure of spinach nitrite reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009507 | cellular_component | chloroplast |
| A | 0010167 | biological_process | response to nitrate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048307 | molecular_function | ferredoxin-nitrite reductase activity |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 563 |
| Chain | Residue |
| A | CYS441 |
| A | CYS447 |
| A | ALA450 |
| A | THR480 |
| A | GLY481 |
| A | CYS482 |
| A | ASN484 |
| A | CYS486 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SRM A 564 |
| Chain | Residue |
| A | ARG109 |
| A | THR141 |
| A | THR142 |
| A | ARG143 |
| A | ASN145 |
| A | GLN147 |
| A | ARG149 |
| A | ARG223 |
| A | LYS224 |
| A | ASN226 |
| A | PHE264 |
| A | PHE265 |
| A | SER266 |
| A | GLN306 |
| A | ARG309 |
| A | GLN402 |
| A | CYS441 |
| A | THR442 |
| A | ASN484 |
| A | CYS486 |
| A | GLN488 |
| A | ARG98 |
Functional Information from PROSITE/UniProt
| site_id | PS00365 |
| Number of Residues | 17 |
| Details | NIR_SIR Nitrite and sulfite reductases iron-sulfur/siroheme-binding site. TGCpnsCgqvqvaDIGF |
| Chain | Residue | Details |
| A | THR480-PHE496 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 323 |
| Chain | Residue | Details |
| A | ARG109 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG223 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS224 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | GLY481 | steric role |
| A | CYS486 | covalently attached |
| A | GLY487 | steric role |
