2NYA
Crystal structure of the periplasmic nitrate reductase (NAP) from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein 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 | 0009061 | biological_process | anaerobic respiration |
| 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 | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| 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 |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
| F | 0008940 | molecular_function | nitrate reductase activity |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0009061 | biological_process | anaerobic respiration |
| F | 0009325 | cellular_component | nitrate reductase complex |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030151 | molecular_function | molybdenum ion binding |
| F | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| F | 0042128 | biological_process | nitrate assimilation |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0043546 | molecular_function | molybdopterin cofactor binding |
| F | 0045333 | biological_process | cellular respiration |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050140 | molecular_function | nitrate reductase (cytochrome) activity |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A 2001 |
| Chain | Residue |
| A | CYS10 |
| A | PHE12 |
| A | CYS13 |
| A | CYS17 |
| A | CYS45 |
| A | LYS47 |
| A | GLY48 |
| A | PRO185 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 6MO A 2002 |
| Chain | Residue |
| A | MGD3001 |
| A | MGD4001 |
| A | HOH4003 |
| A | CYS143 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE MGD A 3001 |
| Chain | Residue |
| A | ARG11 |
| A | GLN114 |
| A | ASN139 |
| A | CYS143 |
| A | GLN340 |
| A | GLN374 |
| A | CYS444 |
| A | THR445 |
| A | ASN446 |
| A | ALA450 |
| A | SER472 |
| A | ASP473 |
| A | PRO474 |
| A | THR477 |
| A | THR489 |
| A | ALA490 |
| A | MET491 |
| A | LYS495 |
| A | ASP522 |
| A | THR682 |
| A | GLY683 |
| A | ARG684 |
| A | TRP689 |
| A | HIS690 |
| A | THR691 |
| A | SER693 |
| A | PHE758 |
| A | ASN766 |
| A | PHE782 |
| A | LYS783 |
| A | 6MO2002 |
| A | MGD4001 |
| A | HOH4032 |
| A | HOH4188 |
| A | HOH4231 |
| site_id | AC4 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE MGD A 4001 |
| Chain | Residue |
| A | CYS13 |
| A | LYS47 |
| A | CYS143 |
| A | TRP176 |
| A | GLY177 |
| A | ASN179 |
| A | GLU182 |
| A | MET183 |
| A | SER207 |
| A | THR208 |
| A | TYR209 |
| A | HIS211 |
| A | PHE223 |
| A | GLN226 |
| A | ASP228 |
| A | THR335 |
| A | MET336 |
| A | GLY337 |
| A | PHE338 |
| A | GLY373 |
| A | GLN374 |
| A | SER681 |
| A | GLY683 |
| A | ARG684 |
| A | VAL685 |
| A | LEU686 |
| A | HIS688 |
| A | TRP689 |
| A | HIS690 |
| A | TYR755 |
| A | LYS783 |
| A | LYS784 |
| A | 6MO2002 |
| A | MGD3001 |
| A | HOH4016 |
| A | HOH4039 |
| A | HOH4123 |
| A | HOH4151 |
| A | HOH4250 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 F 5001 |
| Chain | Residue |
| F | CYS10 |
| F | PHE12 |
| F | CYS13 |
| F | CYS17 |
| F | CYS45 |
| F | LYS47 |
| F | GLY48 |
| F | PRO185 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 6MO F 5002 |
| Chain | Residue |
| F | CYS143 |
| F | MGD6001 |
| F | MGD7001 |
| F | HOH7035 |
| site_id | AC7 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE MGD F 6001 |
| Chain | Residue |
| F | GLN114 |
| F | ASN139 |
| F | CYS143 |
| F | GLN340 |
| F | GLN374 |
| F | CYS444 |
| F | THR445 |
| F | ASN446 |
| F | ALA450 |
| F | SER472 |
| F | ASP473 |
| F | PRO474 |
| F | THR477 |
| F | THR489 |
| F | ALA490 |
| F | MET491 |
| F | LYS495 |
| F | ASP522 |
| F | THR682 |
| F | GLY683 |
| F | ARG684 |
| F | TRP689 |
| F | HIS690 |
| F | THR691 |
| F | SER693 |
| F | PHE758 |
| F | ASN766 |
| F | PHE782 |
| F | LYS783 |
| F | 6MO5002 |
| F | MGD7001 |
| F | HOH7064 |
| F | HOH7242 |
| F | ARG11 |
| site_id | AC8 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE MGD F 7001 |
| Chain | Residue |
| F | CYS13 |
| F | LYS47 |
| F | CYS143 |
| F | TRP176 |
| F | GLY177 |
| F | ASN179 |
| F | GLU182 |
| F | MET183 |
| F | SER207 |
| F | THR208 |
| F | TYR209 |
| F | HIS211 |
| F | PHE223 |
| F | GLN226 |
| F | ASP228 |
| F | THR335 |
| F | MET336 |
| F | GLY337 |
| F | PHE338 |
| F | GLY373 |
| F | GLN374 |
| F | SER681 |
| F | GLY683 |
| F | ARG684 |
| F | VAL685 |
| F | LEU686 |
| F | HIS688 |
| F | TRP689 |
| F | HIS690 |
| F | TYR755 |
| F | LYS783 |
| F | LYS784 |
| F | 6MO5002 |
| F | MGD6001 |
| F | HOH7071 |
| F | HOH7171 |
| F | HOH7259 |
Functional Information from PROSITE/UniProt
| site_id | PS00551 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. ApCrf.CGTgCgVlVgtq.Q |
| Chain | Residue | Details |
| A | ALA8-GLN25 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| 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 | 76 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17130127","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NYA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P81186","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01630","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| A | CYS143 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| F | CYS143 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| A | ARG141 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tmo |
| Chain | Residue | Details |
| F | ARG141 |
