2WPN
Structure of the oxidised, as-isolated NiFeSe hydrogenase from D. vulgaris Hildenborough
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
A | 0009055 | molecular_function | electron transfer activity |
A | 0009061 | biological_process | anaerobic respiration |
A | 0009375 | cellular_component | ferredoxin hydrogenase complex |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
A | 0046872 | molecular_function | metal ion binding |
A | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0005515 | molecular_function | protein binding |
B | 0008901 | molecular_function | ferredoxin hydrogenase activity |
B | 0016151 | molecular_function | nickel cation binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SF4 A 1284 |
Chain | Residue |
A | HIS208 |
A | GLY240 |
A | VAL260 |
A | CYS211 |
A | TYR213 |
A | LEU214 |
A | TYR217 |
A | CYS232 |
A | ARG233 |
A | TYR234 |
A | CYS238 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 A 1285 |
Chain | Residue |
A | THR243 |
A | CYS247 |
A | TRP252 |
A | CYS259 |
A | CYS265 |
A | ILE266 |
A | CYS268 |
B | ARG182 |
B | GLN187 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FSX A 1287 |
Chain | Residue |
A | CYS18 |
A | THR19 |
A | GLY20 |
A | CYS21 |
A | GLU77 |
A | GLY119 |
A | THR120 |
A | CYS121 |
A | GLY158 |
A | CYS159 |
A | PRO160 |
A | HOH2031 |
B | HIS185 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SF4 A 1286 |
Chain | Residue |
A | GLY17 |
A | CYS18 |
A | CYS21 |
A | GLY119 |
A | THR120 |
A | CYS121 |
A | GLY158 |
A | CYS159 |
A | PRO160 |
B | ARG73 |
B | HIS185 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SBY A 1288 |
Chain | Residue |
A | SER22 |
A | LEU37 |
B | GLU167 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SBY A 1289 |
Chain | Residue |
A | PHE73 |
A | VAL170 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FCO B 1497 |
Chain | Residue |
B | CYS78 |
B | HIS82 |
B | ALA420 |
B | PRO421 |
B | ARG422 |
B | LEU425 |
B | ALA444 |
B | SER445 |
B | PSW489 |
B | CYS492 |
B | NI1498 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI B 1498 |
Chain | Residue |
B | CYS78 |
B | PSW489 |
B | CYS492 |
B | FCO1497 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B 1499 |
Chain | Residue |
B | GLU56 |
B | ILE441 |
B | HIS495 |
B | HOH2031 |
B | HOH2119 |
B | HOH2120 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL B 1500 |
Chain | Residue |
B | CYS78 |
B | THR80 |
B | ALA81 |
B | PHE110 |
B | ASN113 |
B | PRO421 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SBY B 1501 |
Chain | Residue |
B | GLN128 |
B | VAL131 |
B | PRO134 |
B | PHE139 |
B | TYR162 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SBY B 1502 |
Chain | Residue |
B | TYR162 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGFEtilrgrdprdasqivQRiCGVC |
Chain | Residue | Details |
B | ARG53-CYS78 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPULGCav.H |
Chain | Residue | Details |
B | PHE486-HIS495 |