3IR6
Crystal structure of NarGHI mutant NarG-H49S
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 | 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 | 0160182 | molecular_function | nitrate reductase (quinone) activity |
| 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 |
| B | 0160182 | molecular_function | nitrate reductase (quinone) activity |
| 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 | 0020037 | molecular_function | heme binding |
| C | 0042126 | biological_process | nitrate metabolic process |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0044799 | cellular_component | NarGHI complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0160182 | molecular_function | nitrate reductase (quinone) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP A 1247 |
| Chain | Residue |
| A | PHE188 |
| A | ASP772 |
| A | PHE773 |
| A | ARG774 |
| A | THR788 |
| A | TRP791 |
| A | LYS794 |
| A | ASP822 |
| A | HIS1098 |
| A | SER1099 |
| A | THR1100 |
| A | PRO190 |
| A | TYR220 |
| A | ARG713 |
| A | SER714 |
| A | ASN715 |
| A | SER719 |
| A | SER720 |
| A | LEU771 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP A 1248 |
| Chain | Residue |
| A | TRP252 |
| A | GLY253 |
| A | ASN255 |
| A | THR259 |
| A | VAL280 |
| A | PRO282 |
| A | ASP283 |
| A | ALA285 |
| A | GLY300 |
| A | ASP302 |
| A | GLY541 |
| A | ALA542 |
| A | GLY543 |
| A | LEU544 |
| A | TRP547 |
| A | TYR577 |
| A | PRO1091 |
| A | HIS1092 |
| A | ARG1218 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AGA A 1249 |
| Chain | Residue |
| A | PHE3 |
| A | ARG6 |
| A | HOH1290 |
| B | ARG218 |
| C | TRP25 |
| C | TYR28 |
| C | TRP207 |
| C | SER208 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B 802 |
| Chain | Residue |
| B | CYS16 |
| B | ILE17 |
| B | CYS19 |
| B | HIS20 |
| B | CYS22 |
| B | CYS263 |
| B | GLY265 |
| B | ILE267 |
| B | ARG268 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 803 |
| 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 804 |
| 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 | 12 |
| Details | BINDING SITE FOR RESIDUE F3S B 805 |
| Chain | Residue |
| B | CYS196 |
| B | PRO197 |
| B | SER198 |
| B | ILE201 |
| B | CYS217 |
| B | ARG218 |
| B | GLY219 |
| B | TRP220 |
| B | ARG221 |
| B | MET222 |
| B | CYS223 |
| B | SER241 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 806 |
| Chain | Residue |
| C | LEU203 |
| C | HIS205 |
| C | ILE206 |
| C | VAL209 |
| C | HOH228 |
| B | ILE88 |
| B | PHE89 |
| B | TRP220 |
| B | ARG221 |
| C | SER39 |
| C | SER40 |
| C | GLN41 |
| C | MET48 |
| C | PHE55 |
| C | HIS56 |
| C | ILE59 |
| C | ARG112 |
| C | LEU130 |
| C | LEU133 |
| C | ARG202 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM C 807 |
| Chain | Residue |
| C | ILE59 |
| C | ILE62 |
| C | HIS66 |
| C | ALA90 |
| C | GLY94 |
| C | LEU133 |
| C | GLN136 |
| C | CYS137 |
| C | GLY140 |
| C | LEU141 |
| C | SER147 |
| C | MET156 |
| C | LEU159 |
| C | HIS187 |
| C | LEU188 |
| C | GLY191 |
| C | MET192 |
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 | 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 | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 31 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 29 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12910261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725769","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"15919996","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 15 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12910261","evidenceCode":"ECO:0000269"}]} |
| 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 | CYS213 |
