4IUD
Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form with ascorbate - partly reduced state
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 |
S | 0005515 | molecular_function | protein binding |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NFV L 1001 |
Chain | Residue |
L | CYS75 |
L | PRO552 |
L | THR553 |
L | CSO597 |
L | CYS600 |
L | CYS78 |
L | CYS81 |
L | HIS82 |
L | ALA528 |
L | PRO529 |
L | ARG530 |
L | LEU533 |
L | VAL551 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG L 1002 |
Chain | Residue |
L | GLU56 |
L | CYS549 |
L | HIS603 |
L | HOH1660 |
L | HOH1661 |
L | HOH1662 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SF4 S 1001 |
Chain | Residue |
S | HIS187 |
S | CYS190 |
S | ARG193 |
S | CYS215 |
S | LEU216 |
S | CYS221 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE F3S S 1002 |
Chain | Residue |
L | LYS226 |
S | THR226 |
S | ASN228 |
S | CYS230 |
S | TRP235 |
S | PRO242 |
S | CYS249 |
S | ILE250 |
S | CYS252 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE S3F S 1003 |
Chain | Residue |
L | HIS229 |
S | CYS17 |
S | THR18 |
S | CYS19 |
S | CYS20 |
S | GLU76 |
S | SER114 |
S | CYS115 |
S | CYS120 |
S | CYS149 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL S 1004 |
Chain | Residue |
S | TRP118 |
S | CYS120 |
S | GLY256 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEvilkgrdprdawafvERiCGVC |
Chain | Residue | Details |
L | ARG53-CYS78 |
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 | PHE594-HIS603 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 11 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P21853 |
Chain | Residue | Details |
S | CYS17 | |
S | CYS249 | |
S | CYS252 | |
S | CYS20 | |
S | CYS115 | |
S | CYS149 | |
S | HIS187 | |
S | CYS190 | |
S | CYS215 | |
S | CYS221 | |
S | CYS230 |