1R27
Crystal Structure of NarGH complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0019645 | biological_process | anaerobic electron transport chain |
| A | 0042126 | biological_process | nitrate metabolic process |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0044799 | cellular_component | NarGHI complex |
| A | 0045333 | biological_process | cellular respiration |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008940 | molecular_function | nitrate reductase activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009061 | biological_process | anaerobic respiration |
| B | 0009325 | cellular_component | nitrate reductase complex |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019645 | biological_process | anaerobic electron transport chain |
| B | 0042126 | biological_process | nitrate metabolic process |
| B | 0042128 | biological_process | nitrate assimilation |
| B | 0044799 | cellular_component | NarGHI complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008940 | molecular_function | nitrate reductase activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009061 | biological_process | anaerobic respiration |
| C | 0009325 | cellular_component | nitrate reductase complex |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019645 | biological_process | anaerobic electron transport chain |
| C | 0042126 | biological_process | nitrate metabolic process |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0043546 | molecular_function | molybdopterin cofactor binding |
| C | 0044799 | cellular_component | NarGHI complex |
| C | 0045333 | biological_process | cellular respiration |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 1990204 | cellular_component | oxidoreductase complex |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008940 | molecular_function | nitrate reductase activity |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009061 | biological_process | anaerobic respiration |
| D | 0009325 | cellular_component | nitrate reductase complex |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019645 | biological_process | anaerobic electron transport chain |
| D | 0042126 | biological_process | nitrate metabolic process |
| D | 0042128 | biological_process | nitrate assimilation |
| D | 0044799 | cellular_component | NarGHI complex |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MO A 5803 |
| Chain | Residue |
| A | ASP222 |
| A | MGD5801 |
| A | MGD5802 |
| A | HOH6570 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MO C 7803 |
| Chain | Residue |
| C | ASP222 |
| C | MGD7801 |
| C | MGD7802 |
| C | HOH8538 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S B 5808 |
| Chain | Residue |
| B | ILE201 |
| B | CYS217 |
| B | ARG218 |
| B | TRP220 |
| B | ARG221 |
| B | MET222 |
| B | CYS223 |
| B | SER241 |
| B | CYS196 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S D 7808 |
| Chain | Residue |
| D | CYS196 |
| D | ILE201 |
| D | CYS217 |
| D | ARG218 |
| D | TRP220 |
| D | ARG221 |
| D | MET222 |
| D | CYS223 |
| D | SER241 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 5800 |
| Chain | Residue |
| B | CYS26 |
| B | ASN42 |
| B | CYS244 |
| B | ILE245 |
| B | PHE246 |
| B | CYS247 |
| B | THR257 |
| B | CYS259 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 5805 |
| Chain | Residue |
| B | CYS184 |
| B | GLU185 |
| B | CYS187 |
| B | ALA191 |
| B | CYS192 |
| B | CYS227 |
| B | TYR229 |
| B | ILE232 |
| B | LYS243 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 5806 |
| Chain | Residue |
| B | CYS16 |
| B | GLY18 |
| B | CYS19 |
| B | HIS20 |
| B | CYS22 |
| B | CYS263 |
| B | GLY265 |
| B | ILE267 |
| B | ARG268 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 5807 |
| Chain | Residue |
| A | HIS49 |
| A | VAL51 |
| A | CYS53 |
| A | GLY55 |
| A | SER56 |
| A | CYS57 |
| A | TRP59 |
| A | GLY91 |
| A | CYS92 |
| A | TYR1101 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 7800 |
| Chain | Residue |
| D | CYS26 |
| D | TRP30 |
| D | ASN42 |
| D | CYS244 |
| D | ILE245 |
| D | PHE246 |
| D | CYS247 |
| D | THR257 |
| D | CYS259 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 7805 |
| Chain | Residue |
| D | CYS184 |
| D | GLU185 |
| D | CYS187 |
| D | ALA191 |
| D | CYS192 |
| D | CYS227 |
| D | TYR229 |
| D | ILE232 |
| D | LYS243 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D 7806 |
| Chain | Residue |
| D | CYS16 |
| D | CYS19 |
| D | HIS20 |
| D | CYS22 |
| D | CYS263 |
| D | VAL264 |
| D | GLY265 |
| D | ILE267 |
| D | ARG268 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C 7807 |
| Chain | Residue |
| C | TYR1101 |
| C | HIS49 |
| C | VAL51 |
| C | CYS53 |
| C | GLY55 |
| C | SER56 |
| C | CYS57 |
| C | TRP59 |
| C | GLY91 |
| C | CYS92 |
| C | GLY95 |
| site_id | BC4 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE MGD A 5801 |
| Chain | Residue |
| A | GLY50 |
| A | ASN52 |
| A | PRO190 |
| A | TYR220 |
| A | ASP222 |
| A | HIS546 |
| A | TRP712 |
| A | ARG713 |
| A | SER714 |
| A | ASN715 |
| A | SER720 |
| A | LYS722 |
| A | LEU771 |
| A | ASP772 |
| A | PHE773 |
| A | ARG774 |
| A | THR788 |
| A | TRP791 |
| A | LYS794 |
| A | ASP822 |
| A | THR1090 |
| A | HIS1092 |
| A | ILE1097 |
| A | HIS1098 |
| A | SER1099 |
| A | THR1100 |
| A | HIS1163 |
| A | ASN1185 |
| A | ASN1217 |
| A | ARG1218 |
| A | MGD5802 |
| A | MO5803 |
| A | HOH5995 |
| A | HOH6018 |
| A | HOH6058 |
| A | HOH6090 |
| A | HOH6135 |
| A | HOH6568 |
| A | HOH6570 |
| A | HOH6580 |
| site_id | BC5 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE MGD A 5802 |
| Chain | Residue |
| A | ASN52 |
| A | ARG94 |
| A | ASP222 |
| A | TRP252 |
| A | GLY253 |
| A | ASN255 |
| A | GLN258 |
| A | THR259 |
| A | VAL280 |
| A | THR281 |
| A | PRO282 |
| A | ASP283 |
| A | ALA285 |
| A | GLN299 |
| A | GLY300 |
| A | ASP302 |
| A | GLY541 |
| A | ALA542 |
| A | GLY543 |
| A | LEU544 |
| A | TRP547 |
| A | TYR577 |
| A | VAL578 |
| A | GLY579 |
| A | PRO1091 |
| A | HIS1092 |
| A | GLN1093 |
| A | GLY1096 |
| A | ILE1097 |
| A | HIS1098 |
| A | ARG1218 |
| A | MGD5801 |
| A | MO5803 |
| A | HOH5875 |
| A | HOH5889 |
| A | HOH5923 |
| A | HOH6075 |
| A | HOH6577 |
| A | HOH6615 |
| site_id | BC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE MGD C 7801 |
| Chain | Residue |
| C | GLY50 |
| C | ASN52 |
| C | PRO190 |
| C | TYR220 |
| C | ASP222 |
| C | HIS546 |
| C | ARG713 |
| C | SER714 |
| C | ASN715 |
| C | SER720 |
| C | LYS722 |
| C | LEU771 |
| C | ASP772 |
| C | PHE773 |
| C | ARG774 |
| C | THR788 |
| C | TRP791 |
| C | LYS794 |
| C | ASP822 |
| C | THR1090 |
| C | HIS1092 |
| C | ILE1097 |
| C | HIS1098 |
| C | SER1099 |
| C | THR1100 |
| C | HIS1163 |
| C | HIS1184 |
| C | ASN1185 |
| C | ASN1217 |
| C | ARG1218 |
| C | MGD7802 |
| C | MO7803 |
| C | HOH7861 |
| C | HOH7908 |
| C | HOH8037 |
| C | HOH8108 |
| C | HOH8538 |
| C | HOH8539 |
| site_id | BC7 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE MGD C 7802 |
| Chain | Residue |
| C | ASN52 |
| C | ARG94 |
| C | ASP222 |
| C | TRP252 |
| C | GLY253 |
| C | ASN255 |
| C | GLN258 |
| C | THR259 |
| C | VAL280 |
| C | THR281 |
| C | PRO282 |
| C | ASP283 |
| C | ALA285 |
| C | GLN299 |
| C | GLY300 |
| C | ASP302 |
| C | GLY541 |
| C | ALA542 |
| C | GLY543 |
| C | LEU544 |
| C | TRP547 |
| C | TYR577 |
| C | VAL578 |
| C | GLY579 |
| C | PRO1091 |
| C | HIS1092 |
| C | GLN1093 |
| C | GLY1096 |
| C | ILE1097 |
| C | HIS1098 |
| C | ARG1218 |
| C | MGD7801 |
| C | MO7803 |
| C | HOH7833 |
| C | HOH7865 |
| C | HOH7970 |
| C | HOH8022 |
| C | HOH8129 |
Functional Information from PROSITE/UniProt
| site_id | PS00490 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. SsTClySDIILPtATwyE |
| Chain | Residue | Details |
| A | SER776-GLU793 |
| site_id | PS00551 |
| Number of Residues | 19 |
| Details | MOLYBDOPTERIN_PROK_1 Prokaryotic molybdopterin oxidoreductases signature 1. StHgvnCTGsCsWkIyvk.N |
| Chain | Residue | Details |
| A | SER47-ASN65 |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AkdlGIaDnDwIeVfNsnGaltarAvVS |
| Chain | Residue | Details |
| A | ALA1124-SER1151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769 |
| Chain | Residue | Details |
| B | CYS16 | |
| B | CYS223 | |
| B | CYS227 | |
| B | CYS244 | |
| B | CYS247 | |
| B | CYS259 | |
| B | CYS263 | |
| D | CYS16 | |
| D | CYS19 | |
| D | CYS22 | |
| D | CYS26 | |
| B | CYS19 | |
| D | CYS184 | |
| D | CYS187 | |
| D | CYS192 | |
| D | CYS196 | |
| D | CYS217 | |
| D | CYS223 | |
| D | CYS227 | |
| D | CYS244 | |
| D | CYS247 | |
| D | CYS259 | |
| B | CYS22 | |
| D | CYS263 | |
| B | CYS26 | |
| B | CYS184 | |
| B | CYS187 | |
| B | CYS192 | |
| B | CYS196 | |
| B | CYS217 |
