4OMF
The F420-reducing [NiFe]-hydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
A | 0016151 | molecular_function | nickel cation binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050454 | molecular_function | coenzyme F420 hydrogenase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016151 | molecular_function | nickel cation binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050454 | molecular_function | coenzyme F420 hydrogenase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
G | 0016151 | molecular_function | nickel cation binding |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0050454 | molecular_function | coenzyme F420 hydrogenase activity |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0051536 | molecular_function | iron-sulfur cluster binding |
G | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 G 301 |
Chain | Residue |
A | HIS150 |
G | GLY56 |
G | CYS57 |
G | ASP60 |
G | SER131 |
G | CYS132 |
G | PHE138 |
G | GLY170 |
G | CYS171 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 G 302 |
Chain | Residue |
G | GLY207 |
G | CYS230 |
G | THR232 |
G | LEU235 |
G | LEU244 |
G | CYS249 |
G | ILE250 |
G | CYS252 |
G | GLY253 |
G | CYS255 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 G 303 |
Chain | Residue |
G | CYS220 |
G | ILE221 |
G | GLY222 |
G | CYS223 |
G | GLY224 |
G | CYS226 |
G | CYS259 |
G | PRO260 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DTZ G 304 |
Chain | Residue |
G | CYS206 |
G | CYS206 |
G | CYS208 |
G | CYS208 |
G | LYS251 |
G | HOH565 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | GLU233 |
A | HOH666 |
A | HOH707 |
G | ALA148 |
G | HOH475 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NFU A 502 |
Chain | Residue |
A | CYS63 |
A | CYS66 |
A | HIS70 |
A | ALA326 |
A | PRO327 |
A | ARG328 |
A | ASP331 |
A | VAL349 |
A | PRO350 |
A | THR351 |
A | CYS380 |
A | CYS383 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 503 |
Chain | Residue |
A | GLU44 |
A | ALA347 |
A | HIS386 |
A | HOH961 |
A | HOH962 |
A | HOH963 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 504 |
Chain | Residue |
A | HOH601 |
A | HOH925 |
A | HOH926 |
A | HOH959 |
A | HOH965 |
A | HOH966 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 505 |
Chain | Residue |
A | ILE156 |
A | ARG308 |
A | HOH683 |
A | HOH699 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SF4 B 401 |
Chain | Residue |
B | ILE102 |
B | PRO103 |
B | CYS104 |
B | CYS134 |
B | MET135 |
B | GLU136 |
B | ASN137 |
B | CYS192 |
B | CYS195 |
B | LYS261 |
G | ILE221 |
G | ARG261 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 402 |
Chain | Residue |
B | HOH501 |
B | HOH570 |
B | HOH626 |
B | HOH660 |
B | HOH694 |
B | HOH695 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE KEN B 403 |
Chain | Residue |
B | ARG110 |
B | GLN113 |
B | ILE126 |
B | ASP204 |
site_id | BC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD B 405 |
Chain | Residue |
B | GLY73 |
B | THR74 |
B | LYS75 |
B | TYR76 |
B | THR77 |
B | SER79 |
B | ASN81 |
B | TYR133 |
B | CYS134 |
B | MET135 |
B | GLU136 |
B | ASN137 |
B | TYR198 |
B | GLY208 |
B | SER209 |
B | VAL210 |
B | HOH507 |
B | HOH514 |
B | HOH591 |
B | HOH619 |
B | ALA23 |
B | GLN24 |
B | ASP25 |
B | GLY26 |
B | GLY27 |
B | ILE28 |
B | VAL29 |
B | THR30 |
B | VAL47 |
B | ALA48 |
B | ALA71 |
Functional Information from PROSITE/UniProt
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiKCGiCYvQCP |
Chain | Residue | Details |
G | CYS249-PRO260 |
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEkmvtgkapetapvmvQRiCGVC |
Chain | Residue | Details |
A | ARG41-CYS66 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. YDPCLSCat.H |
Chain | Residue | Details |
A | TYR377-HIS386 |