5JRD
E. coli Hydrogenase-1 variant P508A
Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0005515 | molecular_function | protein binding |
L | 0005886 | cellular_component | plasma membrane |
L | 0006113 | biological_process | fermentation |
L | 0008901 | molecular_function | ferredoxin hydrogenase activity |
L | 0009055 | molecular_function | electron transfer activity |
L | 0009061 | biological_process | anaerobic respiration |
L | 0009267 | biological_process | cellular response to starvation |
L | 0016020 | cellular_component | membrane |
L | 0016151 | molecular_function | nickel cation binding |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0019645 | biological_process | anaerobic electron transport chain |
L | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
L | 0033748 | molecular_function | hydrogenase (acceptor) activity |
L | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
L | 0046872 | molecular_function | metal ion binding |
L | 0098567 | cellular_component | periplasmic side of plasma membrane |
L | 1902421 | biological_process | hydrogen metabolic process |
M | 0005515 | molecular_function | protein binding |
M | 0005886 | cellular_component | plasma membrane |
M | 0006113 | biological_process | fermentation |
M | 0008901 | molecular_function | ferredoxin hydrogenase activity |
M | 0009055 | molecular_function | electron transfer activity |
M | 0009061 | biological_process | anaerobic respiration |
M | 0009267 | biological_process | cellular response to starvation |
M | 0016020 | cellular_component | membrane |
M | 0016151 | molecular_function | nickel cation binding |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0019645 | biological_process | anaerobic electron transport chain |
M | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
M | 0033748 | molecular_function | hydrogenase (acceptor) activity |
M | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
M | 0046872 | molecular_function | metal ion binding |
M | 0098567 | cellular_component | periplasmic side of plasma membrane |
M | 1902421 | biological_process | hydrogen metabolic process |
S | 0005886 | cellular_component | plasma membrane |
S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
S | 0009055 | molecular_function | electron transfer activity |
S | 0009061 | biological_process | anaerobic respiration |
S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
S | 0016020 | cellular_component | membrane |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0033748 | molecular_function | hydrogenase (acceptor) activity |
S | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
S | 0046872 | molecular_function | metal ion binding |
S | 0051536 | molecular_function | iron-sulfur cluster binding |
S | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
S | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
T | 0005886 | cellular_component | plasma membrane |
T | 0008901 | molecular_function | ferredoxin hydrogenase activity |
T | 0009055 | molecular_function | electron transfer activity |
T | 0009061 | biological_process | anaerobic respiration |
T | 0009375 | cellular_component | ferredoxin hydrogenase complex |
T | 0016020 | cellular_component | membrane |
T | 0016491 | molecular_function | oxidoreductase activity |
T | 0033748 | molecular_function | hydrogenase (acceptor) activity |
T | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
T | 0046872 | molecular_function | metal ion binding |
T | 0051536 | molecular_function | iron-sulfur cluster binding |
T | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
T | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue SF4 S 401 |
Chain | Residue |
S | HIS187 |
S | CYS190 |
S | ARG193 |
S | CYS215 |
S | LEU216 |
S | CYS221 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue F3S S 402 |
Chain | Residue |
S | CYS230 |
S | TRP235 |
S | CYS249 |
S | LEU250 |
S | CYS252 |
L | LYS226 |
S | THR226 |
S | ASN228 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue SF3 S 403 |
Chain | Residue |
L | HOH717 |
S | GLU16 |
S | CYS17 |
S | CYS19 |
S | CYS20 |
S | GLU76 |
S | THR114 |
S | CYS115 |
S | CYS120 |
S | CYS149 |
S | HOH671 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL S 404 |
Chain | Residue |
S | CYS120 |
S | GLY256 |
S | HOH595 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue CL S 405 |
Chain | Residue |
S | ILE12 |
S | HIS13 |
S | ASP46 |
S | LYS98 |
S | HOH549 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue FCO L 601 |
Chain | Residue |
L | CSO79 |
L | VAL82 |
L | HIS83 |
L | ALA507 |
L | ALA508 |
L | ARG509 |
L | VAL530 |
L | PRO531 |
L | THR532 |
L | CYS576 |
L | CYS579 |
L | NI602 |
L | HOH949 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue NI L 602 |
Chain | Residue |
L | CYS76 |
L | CSO79 |
L | CYS576 |
L | CYS579 |
L | FCO601 |
L | HOH949 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MG L 603 |
Chain | Residue |
L | GLU57 |
L | CYS528 |
L | HIS582 |
L | HOH726 |
L | HOH727 |
L | HOH730 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 L 604 |
Chain | Residue |
L | LEU482 |
L | ALA483 |
S | ARG211 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 L 605 |
Chain | Residue |
L | LYS157 |
L | HOH750 |
L | HOH992 |
M | LYS157 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue SF4 T 401 |
Chain | Residue |
T | HIS187 |
T | CYS190 |
T | ARG193 |
T | CYS215 |
T | LEU216 |
T | CYS221 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue F3S T 402 |
Chain | Residue |
M | LYS226 |
T | THR226 |
T | ASN228 |
T | CYS230 |
T | TRP235 |
T | PRO242 |
T | CYS249 |
T | LEU250 |
T | CYS252 |
site_id | AD4 |
Number of Residues | 11 |
Details | binding site for residue SF3 T 403 |
Chain | Residue |
M | HOH720 |
T | GLU16 |
T | CYS17 |
T | CYS19 |
T | CYS20 |
T | GLU76 |
T | THR114 |
T | CYS115 |
T | CYS120 |
T | CYS149 |
T | HOH611 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue CL T 404 |
Chain | Residue |
T | CYS120 |
T | GLY256 |
T | HOH622 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue CL T 405 |
Chain | Residue |
T | HOH673 |
T | ILE12 |
T | HIS13 |
T | ASP46 |
T | LYS98 |
T | HOH570 |
site_id | AD7 |
Number of Residues | 13 |
Details | binding site for residue FCO M 601 |
Chain | Residue |
M | CSO79 |
M | VAL82 |
M | HIS83 |
M | ALA507 |
M | ALA508 |
M | ARG509 |
M | VAL530 |
M | PRO531 |
M | THR532 |
M | CYS576 |
M | CYS579 |
M | NI602 |
M | HOH918 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue NI M 602 |
Chain | Residue |
M | CYS76 |
M | CSO79 |
M | CYS576 |
M | CYS579 |
M | FCO601 |
M | HOH918 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue MG M 603 |
Chain | Residue |
M | GLU57 |
M | CYS528 |
M | HIS582 |
M | HOH715 |
M | HOH718 |
M | HOH733 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue SO4 M 604 |
Chain | Residue |
M | ARG394 |
S | ARG125 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEiilqgrdprdawafvERiCGVC |
Chain | Residue | Details |
L | ARG54-CSO79 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCLACst.H |
Chain | Residue | Details |
L | PHE573-HIS582 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
L | CYS76 | |
L | CSO79 | |
L | CYS576 | |
L | CYS579 | |
M | CYS76 | |
M | CSO79 | |
M | CYS576 | |
M | CYS579 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
S | VAL282-ALA302 | |
T | VAL282-ALA302 |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
S | VAL303-ALA327 | |
T | VAL303-ALA327 |
site_id | SWS_FT_FI4 |
Number of Residues | 22 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P21853 |
Chain | Residue | Details |
S | CYS17 | |
S | CYS249 | |
S | CYS252 | |
T | CYS17 | |
T | CYS20 | |
T | CYS115 | |
T | CYS149 | |
T | HIS187 | |
T | CYS190 | |
T | CYS215 | |
T | CYS221 | |
S | CYS20 | |
T | CYS230 | |
T | CYS249 | |
T | CYS252 | |
S | CYS115 | |
S | CYS149 | |
S | HIS187 | |
S | CYS190 | |
S | CYS215 | |
S | CYS221 | |
S | CYS230 |