3ML1
Crystal Structure of the Periplasmic Nitrate Reductase from Cupriavidus necator
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| A | 0008940 | molecular_function | nitrate reductase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009325 | cellular_component | nitrate reductase complex |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0045333 | biological_process | cellular respiration |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 1990204 | cellular_component | oxidoreductase complex |
| B | 0009061 | biological_process | anaerobic respiration |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1801 |
| Chain | Residue |
| A | CYS19 |
| A | PRO194 |
| A | ILE195 |
| A | PHE21 |
| A | CYS22 |
| A | GLY25 |
| A | CYS26 |
| A | ASN53 |
| A | CYS54 |
| A | LYS56 |
| A | GLY57 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MOS A 1802 |
| Chain | Residue |
| A | CYS152 |
| A | GLN384 |
| A | ARG694 |
| A | MGD1803 |
| A | MGD1804 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE MGD A 1803 |
| Chain | Residue |
| A | ARG20 |
| A | GLN123 |
| A | ASN148 |
| A | CYS152 |
| A | GLN350 |
| A | GLN384 |
| A | VAL454 |
| A | ASN455 |
| A | ASN456 |
| A | ASN457 |
| A | ALA460 |
| A | SER482 |
| A | ASP483 |
| A | THR487 |
| A | SER499 |
| A | ALA500 |
| A | MET501 |
| A | LYS505 |
| A | ASP532 |
| A | THR692 |
| A | ARG694 |
| A | TRP699 |
| A | HIS700 |
| A | SER701 |
| A | SER703 |
| A | TRP768 |
| A | ASN776 |
| A | PHE792 |
| A | LYS793 |
| A | HOH860 |
| A | HOH937 |
| A | HOH991 |
| A | MOS1802 |
| A | MGD1804 |
| site_id | AC4 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE MGD A 1804 |
| Chain | Residue |
| A | CYS22 |
| A | LYS56 |
| A | CYS152 |
| A | TRP185 |
| A | GLY186 |
| A | ASN188 |
| A | GLU191 |
| A | MET192 |
| A | SER216 |
| A | THR217 |
| A | PHE218 |
| A | HIS220 |
| A | PHE232 |
| A | PRO234 |
| A | GLN235 |
| A | ASP237 |
| A | THR345 |
| A | MET346 |
| A | GLY347 |
| A | PHE348 |
| A | GLY383 |
| A | GLN384 |
| A | GLY693 |
| A | ARG694 |
| A | VAL695 |
| A | LEU696 |
| A | HIS698 |
| A | TRP699 |
| A | HIS700 |
| A | LYS793 |
| A | LYS794 |
| A | HOH803 |
| A | HOH871 |
| A | HOH943 |
| A | HOH956 |
| A | HOH985 |
| A | MOS1802 |
| A | MGD1803 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC B 1128 |
| Chain | Residue |
| B | HIS102 |
| B | HOH455 |
| B | HEC1129 |
| B | PRO40 |
| B | PRO43 |
| B | HIS44 |
| B | TYR49 |
| B | ARG57 |
| B | CYS58 |
| B | CYS61 |
| B | HIS62 |
| B | ALA72 |
| B | ILE73 |
| B | CYS98 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC B 1129 |
| Chain | Residue |
| A | ASN53 |
| A | TYR58 |
| B | GLN38 |
| B | ILE73 |
| B | VAL75 |
| B | SER76 |
| B | ILE77 |
| B | THR78 |
| B | HIS79 |
| B | ARG95 |
| B | PHE97 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | HOH141 |
| B | HOH215 |
| B | HOH302 |
| B | HOH353 |
| B | HOH455 |
| B | HOH513 |
| B | HOH553 |
| B | HEC1128 |
Functional Information from PROSITE/UniProt
| site_id | PS00551 |
| Number of Residues | 19 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. ApCrf.CGTgCgVtVavkdN |
| Chain | Residue | Details |
| A | ALA17-ASN35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | Domain: {"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 38 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21419779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ML1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3O5A","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"21419779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ML1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"21419779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ML1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
