6GAM
Structure of E14Q variant of E. coli hydrogenase-2 (as-isolated enzyme)
Functional Information from GO Data
Chain | GOid | namespace | contents |
L | 0005515 | molecular_function | protein binding |
L | 0005886 | cellular_component | plasma membrane |
L | 0008901 | molecular_function | ferredoxin hydrogenase activity |
L | 0016151 | molecular_function | nickel cation binding |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0033748 | molecular_function | hydrogenase (acceptor) activity |
L | 0046872 | molecular_function | metal ion binding |
M | 0005515 | molecular_function | protein binding |
M | 0005886 | cellular_component | plasma membrane |
M | 0008901 | molecular_function | ferredoxin hydrogenase activity |
M | 0016151 | molecular_function | nickel cation binding |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0033748 | molecular_function | hydrogenase (acceptor) activity |
M | 0046872 | molecular_function | metal ion binding |
S | 0008901 | molecular_function | ferredoxin hydrogenase activity |
S | 0009375 | cellular_component | ferredoxin hydrogenase complex |
S | 0051536 | molecular_function | iron-sulfur cluster binding |
T | 0008901 | molecular_function | ferredoxin hydrogenase activity |
T | 0009375 | cellular_component | ferredoxin hydrogenase complex |
T | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue SF4 S 401 |
Chain | Residue |
S | HIS192 |
S | CYS195 |
S | ARG197 |
S | ARG198 |
S | CYS220 |
S | LEU221 |
S | TYR222 |
S | CYS226 |
S | GLY228 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue F3S S 402 |
Chain | Residue |
L | LYS211 |
L | GLN216 |
S | CYS235 |
S | PHE240 |
S | CYS255 |
S | TYR256 |
S | GLY257 |
S | CYS258 |
S | ASN259 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue SF4 S 403 |
Chain | Residue |
L | ARG59 |
S | CYS22 |
S | CYS25 |
S | GLY118 |
S | SER119 |
S | CYS120 |
S | GLY153 |
S | CYS154 |
S | PRO155 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue FCO L 601 |
Chain | Residue |
L | CYS64 |
L | THR67 |
L | HIS68 |
L | ALA477 |
L | PRO478 |
L | ARG479 |
L | LEU482 |
L | VAL500 |
L | PRO501 |
L | SER502 |
L | CYS549 |
L | NI602 |
L | HOH1041 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NI L 602 |
Chain | Residue |
L | CYS61 |
L | CYS64 |
L | CYS546 |
L | CYS549 |
L | FCO601 |
L | HOH1041 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG L 603 |
Chain | Residue |
L | GLU42 |
L | ALA498 |
L | HIS552 |
L | HOH726 |
L | HOH732 |
L | HOH739 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SF4 T 401 |
Chain | Residue |
T | HIS192 |
T | CYS195 |
T | ARG197 |
T | ARG198 |
T | CYS220 |
T | LEU221 |
T | TYR222 |
T | CYS226 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue F3S T 402 |
Chain | Residue |
M | LYS211 |
M | GLN216 |
T | CYS235 |
T | PHE240 |
T | CYS255 |
T | TYR256 |
T | GLY257 |
T | CYS258 |
T | ASN259 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue SF4 T 403 |
Chain | Residue |
M | ARG59 |
T | CYS22 |
T | CYS25 |
T | GLY118 |
T | SER119 |
T | CYS120 |
T | GLY153 |
T | CYS154 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue FCO M 601 |
Chain | Residue |
M | CYS64 |
M | THR67 |
M | HIS68 |
M | ALA477 |
M | PRO478 |
M | ARG479 |
M | LEU482 |
M | VAL500 |
M | PRO501 |
M | SER502 |
M | CYS549 |
M | NI602 |
M | HOH973 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue NI M 602 |
Chain | Residue |
M | CYS61 |
M | CYS64 |
M | CYS546 |
M | CYS549 |
M | FCO601 |
M | HOH973 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MG M 603 |
Chain | Residue |
M | HOH726 |
M | HOH750 |
M | HOH753 |
M | GLU42 |
M | ALA498 |
M | HIS552 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGMEeivknrdprdawmivQRiCGVC |
Chain | Residue | Details |
L | ARG39-CYS64 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCMACav.H |
Chain | Residue | Details |
L | PHE543-HIS552 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
L | CYS61 | |
S | CYS255 | |
S | CYS258 | |
T | CYS22 | |
T | CYS25 | |
T | CYS120 | |
T | CYS154 | |
T | HIS192 | |
T | CYS195 | |
T | CYS220 | |
T | CYS226 | |
L | CYS64 | |
T | CYS235 | |
T | CYS255 | |
T | CYS258 | |
L | CYS546 | |
L | CYS549 | |
M | CYS61 | |
M | CYS64 | |
M | CYS546 | |
M | CYS549 | |
S | CYS235 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Cleavage; by HybD |
Chain | Residue | Details |
L | HIS552 | |
M | HIS552 |