1E3D
[NiFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 27774
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 |
C | 0008901 | molecular_function | ferredoxin hydrogenase activity |
C | 0009055 | molecular_function | electron transfer activity |
C | 0009061 | biological_process | anaerobic respiration |
C | 0009375 | cellular_component | ferredoxin hydrogenase complex |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0042597 | cellular_component | periplasmic space |
C | 0044569 | cellular_component | [Ni-Fe] hydrogenase complex |
C | 0046872 | molecular_function | metal ion binding |
C | 0047806 | molecular_function | cytochrome-c3 hydrogenase activity |
C | 0051536 | molecular_function | iron-sulfur cluster binding |
C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
D | 0016151 | molecular_function | nickel cation binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 901 |
Chain | Residue |
B | GLU52 |
B | LEU488 |
B | HIS542 |
B | HOH2070 |
B | HOH2355 |
B | HOH2358 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 901 |
Chain | Residue |
D | HOH2043 |
D | HOH2299 |
D | HOH2300 |
D | GLU52 |
D | LEU488 |
D | HIS542 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S A 267 |
Chain | Residue |
A | ASN228 |
A | CYS230 |
A | PHE235 |
A | TRP240 |
A | PRO241 |
A | CYS248 |
A | ILE249 |
A | CYS251 |
B | LYS222 |
B | GLN227 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SF4 A 268 |
Chain | Residue |
A | HIS187 |
A | CYS190 |
A | ARG192 |
A | ARG193 |
A | CYS215 |
A | LEU216 |
A | CYS221 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FSX A 269 |
Chain | Residue |
A | GLU16 |
A | CYS17 |
A | THR18 |
A | GLY19 |
A | CYS20 |
A | GLU75 |
A | THR113 |
A | CYS114 |
A | GLY149 |
A | CYS150 |
A | PRO151 |
A | HOH2122 |
B | HIS225 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE FNE B 543 |
Chain | Residue |
B | CYS71 |
B | CYS74 |
B | HIS78 |
B | VAL467 |
B | SER468 |
B | ARG469 |
B | LEU472 |
B | VAL490 |
B | PRO491 |
B | THR492 |
B | CYS536 |
B | CYS539 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE F3S C 267 |
Chain | Residue |
C | THR226 |
C | ASN228 |
C | CYS230 |
C | PHE235 |
C | TRP240 |
C | CYS248 |
C | ILE249 |
C | CYS251 |
D | LYS222 |
D | GLN227 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SF4 C 268 |
Chain | Residue |
C | HIS187 |
C | CYS190 |
C | ARG192 |
C | ARG193 |
C | CYS215 |
C | LEU216 |
C | CYS221 |
C | VAL242 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE FSX C 269 |
Chain | Residue |
C | GLU16 |
C | CYS17 |
C | THR18 |
C | GLY19 |
C | CYS20 |
C | GLU75 |
C | THR113 |
C | CYS114 |
C | GLY149 |
C | CYS150 |
C | PRO151 |
D | HIS225 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FNE D 543 |
Chain | Residue |
D | CYS71 |
D | CYS74 |
D | HIS78 |
D | VAL467 |
D | ARG469 |
D | LEU472 |
D | VAL490 |
D | PRO491 |
D | THR492 |
D | CYS536 |
D | CYS539 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE H2S A 904 |
Chain | Residue |
A | GLY119 |
A | ASN255 |
A | HOH2124 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE H2S C 904 |
Chain | Residue |
C | GLY119 |
C | ASN255 |
C | HOH2101 |
C | TYR117 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE H2S D 904 |
Chain | Residue |
D | LEU106 |
D | GLN109 |
D | PHE110 |
D | VAL467 |
D | SER468 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE H2S B 904 |
Chain | Residue |
B | LEU106 |
B | PHE110 |
B | VAL467 |
B | SER468 |
Functional Information from PROSITE/UniProt
site_id | PS00507 |
Number of Residues | 26 |
Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGIEtilkgrdprdaqhftQRtCGVC |
Chain | Residue | Details |
B | ARG49-CYS74 |
site_id | PS00508 |
Number of Residues | 10 |
Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCIACst.H |
Chain | Residue | Details |
B | PHE533-HIS542 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cc1 |
Chain | Residue | Details |
A | THR18 | |
B | CYS536 | |
B | GLU24 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cc1 |
Chain | Residue | Details |
C | THR18 | |
D | CYS536 | |
D | GLU24 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1cc1 |
Chain | Residue | Details |
B | CYS536 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1cc1 |
Chain | Residue | Details |
D | CYS536 |