3O5A
Crystal Structure of partially reduced Periplasmic Nitrate Reductase from Cupriavidus necator using Ionic Liquids
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 | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1801 |
| Chain | Residue |
| A | CYS19 |
| A | PHE21 |
| A | CYS22 |
| A | GLY25 |
| A | CYS26 |
| A | ASN53 |
| A | CYS54 |
| A | GLY57 |
| A | PRO194 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MOS A 1802 |
| Chain | Residue |
| A | CYS152 |
| A | GLN384 |
| A | MGD1803 |
| A | MGD1804 |
| site_id | AC3 |
| Number of Residues | 35 |
| 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 | ALA484 |
| 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 | HOH820 |
| A | HOH826 |
| A | HOH860 |
| A | MOS1802 |
| A | MGD1804 |
| site_id | AC4 |
| Number of Residues | 37 |
| 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 | 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 | HOH871 |
| A | HOH888 |
| A | HOH894 |
| A | HOH940 |
| A | HOH1030 |
| A | MOS1802 |
| A | MGD1803 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 803 |
| Chain | Residue |
| A | PHE397 |
| A | HIS399 |
| A | ARG400 |
| A | HOH1090 |
| A | HOH1200 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 804 |
| Chain | Residue |
| A | LEU241 |
| A | ASN242 |
| A | ALA245 |
| A | MET360 |
| A | ASN363 |
| A | LEU364 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT A 805 |
| Chain | Residue |
| A | TYR587 |
| A | FMT815 |
| A | HOH883 |
| A | HOH1216 |
| A | SER15 |
| A | LYS16 |
| A | HIS520 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 806 |
| Chain | Residue |
| A | ARG150 |
| A | HIS399 |
| A | ILE786 |
| A | HOH1279 |
| A | HOH1297 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A 807 |
| Chain | Residue |
| A | ASP167 |
| A | GLU168 |
| A | ARG392 |
| A | GLU393 |
| A | ASP404 |
| A | HIS616 |
| A | TRP632 |
| A | HOH817 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 809 |
| Chain | Residue |
| A | ARG734 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 810 |
| Chain | Residue |
| A | ALA627 |
| A | ARG628 |
| A | HOH1361 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 811 |
| Chain | Residue |
| A | GLY229 |
| A | ILE230 |
| A | ILE231 |
| A | LYS325 |
| A | HOH1126 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 812 |
| Chain | Residue |
| A | ARG203 |
| A | HOH1322 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 813 |
| Chain | Residue |
| A | ARG733 |
| A | ARG734 |
| A | HOH1408 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 814 |
| Chain | Residue |
| A | GLY527 |
| A | GLU528 |
| A | ALA529 |
| A | ARG530 |
| A | HOH960 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 815 |
| Chain | Residue |
| A | GLU626 |
| A | FMT805 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 816 |
| Chain | Residue |
| A | SER772 |
| A | LEU774 |
| A | LYS777 |
| B | ARG7 |
| site_id | BC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC B 1128 |
| Chain | Residue |
| B | PRO40 |
| B | THR41 |
| B | ILE42 |
| B | PRO43 |
| B | HIS44 |
| B | ILE46 |
| B | TYR49 |
| B | ARG57 |
| B | CYS58 |
| B | CYS61 |
| B | HIS62 |
| B | ALA72 |
| B | ILE73 |
| B | CYS98 |
| B | HIS102 |
| B | FMT140 |
| B | HOH355 |
| B | HOH667 |
| site_id | CC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC B 1129 |
| Chain | Residue |
| A | ASN53 |
| A | TYR58 |
| B | GLN38 |
| B | PRO39 |
| B | PRO40 |
| B | ILE73 |
| B | VAL75 |
| B | SER76 |
| B | THR78 |
| B | HIS79 |
| B | ARG95 |
| B | PHE97 |
| B | CYS98 |
| B | CYS101 |
| B | HIS102 |
| B | HOH162 |
| B | HOH409 |
| B | HOH568 |
| B | HOH667 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 135 |
| Chain | Residue |
| B | GLY48 |
| B | TYR49 |
| B | GLN50 |
| B | ARG57 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 136 |
| Chain | Residue |
| A | LYS109 |
| A | ARG746 |
| B | ALA13 |
| B | ASN14 |
| B | GLU15 |
| B | HOH144 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 137 |
| Chain | Residue |
| B | GLY113 |
| B | ASN114 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 138 |
| Chain | Residue |
| B | LEU2 |
| B | VAL3 |
| B | HOH767 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 139 |
| Chain | Residue |
| A | LEU491 |
| B | VAL3 |
| B | ASP4 |
| B | ARG7 |
| B | GLY8 |
| B | HOH684 |
| B | HOH710 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 140 |
| Chain | Residue |
| B | HIS44 |
| B | TYR49 |
| 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 |
