3UQY
H2-reduced structure of E. coli hydrogenase-1
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 | 0005515 | molecular_function | protein binding |
S | 0005886 | cellular_component | plasma membrane |
S | 0006113 | biological_process | fermentation |
S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
S | 0009055 | molecular_function | electron transfer activity |
S | 0009061 | biological_process | anaerobic respiration |
S | 0009267 | biological_process | cellular response to starvation |
S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
S | 0016020 | cellular_component | membrane |
S | 0016491 | molecular_function | oxidoreductase activity |
S | 0019645 | biological_process | anaerobic electron transport chain |
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 |
S | 0098567 | cellular_component | periplasmic side of plasma membrane |
S | 1902421 | biological_process | hydrogen metabolic process |
T | 0005515 | molecular_function | protein binding |
T | 0005886 | cellular_component | plasma membrane |
T | 0006113 | biological_process | fermentation |
T | 0008901 | molecular_function | ferredoxin hydrogenase activity |
T | 0009055 | molecular_function | electron transfer activity |
T | 0009061 | biological_process | anaerobic respiration |
T | 0009267 | biological_process | cellular response to starvation |
T | 0009375 | cellular_component | ferredoxin hydrogenase complex |
T | 0016020 | cellular_component | membrane |
T | 0016491 | molecular_function | oxidoreductase activity |
T | 0019645 | biological_process | anaerobic electron transport chain |
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 |
T | 0098567 | cellular_component | periplasmic side of plasma membrane |
T | 1902421 | biological_process | hydrogen metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 S 401 |
Chain | Residue |
S | HIS187 |
S | CYS190 |
S | ARG193 |
S | CYS215 |
S | LEU216 |
S | CYS221 |
S | ILE243 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F3S S 402 |
Chain | Residue |
S | CYS230 |
S | TRP235 |
S | PRO242 |
S | CYS249 |
S | LEU250 |
S | CYS252 |
L | LYS226 |
S | ASN228 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F4S S 403 |
Chain | Residue |
S | CYS17 |
S | THR18 |
S | CYS19 |
S | CYS20 |
S | THR114 |
S | CYS115 |
S | CYS120 |
S | CYS149 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LMT S 404 |
Chain | Residue |
S | ILE7 |
S | TRP11 |
S | ILE72 |
S | MET163 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL S 405 |
Chain | Residue |
S | TRP118 |
S | CYS120 |
S | GLY256 |
S | HOH548 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL S 406 |
Chain | Residue |
M | ARG433 |
S | ASP173 |
S | ARG174 |
S | HOH658 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 S 407 |
Chain | Residue |
L | LEU482 |
L | ALA483 |
S | ARG211 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 S 408 |
Chain | Residue |
S | LYS218 |
S | ARG266 |
S | HOH736 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FCO L 601 |
Chain | Residue |
L | CYS79 |
L | VAL82 |
L | HIS83 |
L | ALA507 |
L | PRO508 |
L | ARG509 |
L | LEU512 |
L | VAL530 |
L | PRO531 |
L | THR532 |
L | CYS576 |
L | CYS579 |
L | NI602 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI L 602 |
Chain | Residue |
L | CYS76 |
L | CYS79 |
L | CYS576 |
L | CYS579 |
L | FCO601 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG L 603 |
Chain | Residue |
L | GLU57 |
L | CYS528 |
L | HIS582 |
L | HOH701 |
L | HOH702 |
L | HOH703 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 L 604 |
Chain | Residue |
L | LYS157 |
L | HOH1030 |
L | HOH1065 |
M | LYS157 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL L 605 |
Chain | Residue |
L | PHE331 |
L | HIS421 |
L | GLN446 |
L | HOH1008 |
L | HOH1056 |
site_id | BC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL L 606 |
Chain | Residue |
L | LEU135 |
L | LEU179 |
L | ASN184 |
L | TRP187 |
L | HOH1142 |
M | GLU488 |
M | LYS489 |
M | THR494 |
M | HOH1085 |
M | HOH1141 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL L 607 |
Chain | Residue |
L | CYS499 |
L | ARG500 |
L | HOH947 |
site_id | BC7 |
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 | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S T 402 |
Chain | Residue |
T | CYS249 |
T | LEU250 |
T | CYS252 |
M | LYS226 |
T | THR226 |
T | ASN228 |
T | CYS230 |
T | TRP235 |
T | PRO242 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE F4S T 403 |
Chain | Residue |
T | CYS17 |
T | THR18 |
T | CYS19 |
T | CYS20 |
T | THR114 |
T | CYS115 |
T | CYS120 |
T | CYS149 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LMT T 404 |
Chain | Residue |
T | ILE7 |
T | TRP11 |
T | ILE160 |
T | MET163 |
T | ASP167 |
T | ARG168 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL T 405 |
Chain | Residue |
T | TRP118 |
T | CYS120 |
T | GLY256 |
T | HOH547 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 T 406 |
Chain | Residue |
T | LYS218 |
T | ARG266 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 T 407 |
Chain | Residue |
L | HOH1219 |
T | ASP173 |
T | ARG174 |
site_id | CC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FCO M 601 |
Chain | Residue |
M | CYS79 |
M | VAL82 |
M | HIS83 |
M | ALA507 |
M | PRO508 |
M | ARG509 |
M | LEU512 |
M | VAL530 |
M | PRO531 |
M | THR532 |
M | CYS576 |
M | CYS579 |
M | NI602 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI M 602 |
Chain | Residue |
M | CYS76 |
M | CYS79 |
M | CYS576 |
M | CYS579 |
M | FCO601 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG M 603 |
Chain | Residue |
M | GLU57 |
M | CYS528 |
M | HIS582 |
M | HOH702 |
M | HOH703 |
M | HOH704 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL M 604 |
Chain | Residue |
M | LEU179 |
M | ASN184 |
M | HOH913 |
M | HOH1115 |
T | HOH733 |
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-CYS79 |
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 | CYS79 | |
L | CYS576 | |
L | CYS579 | |
M | CYS76 | |
M | CYS79 | |
M | CYS576 | |
M | CYS579 |
site_id | SWS_FT_FI2 |
Number of Residues | 44 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
S | THR281-VAL303 | |
T | THR281-VAL303 |
site_id | SWS_FT_FI3 |
Number of Residues | 46 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
S | ASP304-ALA327 | |
T | ASP304-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 |