5Y34
Membrane-bound respiratory [NiFe]-hydrogenase from Hydrogenovibrio marinus in a ferricyanide-oxidized condition
Replaces: 3AYYFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| B | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| C | 0016151 | molecular_function | nickel cation binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0009375 | cellular_component | ferredoxin hydrogenase complex |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue 3NI A 601 |
| Chain | Residue |
| A | CYS76 |
| A | CYS79 |
| A | CYS590 |
| A | CYS593 |
| A | FCO602 |
| A | O603 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue FCO A 602 |
| Chain | Residue |
| A | ALA521 |
| A | PRO522 |
| A | ARG523 |
| A | LEU526 |
| A | VAL544 |
| A | PRO545 |
| A | THR546 |
| A | CYS593 |
| A | 3NI601 |
| A | O603 |
| A | CYS79 |
| A | CYS82 |
| A | HIS83 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue O A 603 |
| Chain | Residue |
| A | CYS79 |
| A | ARG523 |
| A | CYS590 |
| A | CYS593 |
| A | 3NI601 |
| A | FCO602 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | LYS310 |
| A | GLN319 |
| A | ASP482 |
| A | HOH816 |
| A | HOH925 |
| A | HOH1184 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | ILE242 |
| A | ASN243 |
| A | ILE244 |
| A | ASP245 |
| A | GLY246 |
| A | SER496 |
| A | HOH782 |
| A | HOH1336 |
| B | ARG220 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 606 |
| Chain | Residue |
| A | GLU57 |
| A | CYS542 |
| A | HIS596 |
| A | HOH729 |
| A | HOH746 |
| A | HOH752 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue SF3 B 301 |
| Chain | Residue |
| B | CYS23 |
| B | THR24 |
| B | CYS25 |
| B | CYS26 |
| B | GLU82 |
| B | SER120 |
| B | CYS121 |
| B | CYS126 |
| B | GLY157 |
| B | CYS158 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue F3S B 302 |
| Chain | Residue |
| A | LYS227 |
| B | ILE195 |
| B | THR235 |
| B | ASN237 |
| B | CYS239 |
| B | TRP244 |
| B | PRO251 |
| B | CYS258 |
| B | ILE259 |
| B | CYS261 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 B 303 |
| Chain | Residue |
| B | HIS196 |
| B | CYS199 |
| B | ARG202 |
| B | CYS224 |
| B | LEU225 |
| B | CYS230 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 701 |
| Chain | Residue |
| C | GLU57 |
| C | CYS542 |
| C | HIS596 |
| C | HOH817 |
| C | HOH829 |
| C | HOH831 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue 3NI C 702 |
| Chain | Residue |
| C | CYS76 |
| C | CYS79 |
| C | CYS590 |
| C | CYS593 |
| C | FCO703 |
| C | O704 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue FCO C 703 |
| Chain | Residue |
| C | CYS79 |
| C | CYS82 |
| C | HIS83 |
| C | ALA521 |
| C | PRO522 |
| C | ARG523 |
| C | LEU526 |
| C | VAL544 |
| C | PRO545 |
| C | THR546 |
| C | CYS593 |
| C | 3NI702 |
| C | O704 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue O C 704 |
| Chain | Residue |
| C | CYS590 |
| C | CYS593 |
| C | 3NI702 |
| C | FCO703 |
| C | CYS79 |
| C | ARG523 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 705 |
| Chain | Residue |
| C | LYS310 |
| C | GLN319 |
| C | ASP482 |
| C | HOH917 |
| C | HOH1178 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 706 |
| Chain | Residue |
| C | ILE242 |
| C | ASN243 |
| C | ILE244 |
| C | ASP245 |
| C | GLY246 |
| C | SER496 |
| C | HOH812 |
| C | HOH1390 |
| D | ARG220 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue SF3 D 301 |
| Chain | Residue |
| D | CYS23 |
| D | THR24 |
| D | CYS25 |
| D | CYS26 |
| D | GLU82 |
| D | SER120 |
| D | CYS121 |
| D | CYS126 |
| D | GLY157 |
| D | CYS158 |
| site_id | AD8 |
| Number of Residues | 9 |
| Details | binding site for residue F3S D 302 |
| Chain | Residue |
| C | LYS227 |
| D | THR235 |
| D | ASN237 |
| D | CYS239 |
| D | TRP244 |
| D | PRO251 |
| D | CYS258 |
| D | ILE259 |
| D | CYS261 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 D 303 |
| Chain | Residue |
| D | HIS196 |
| D | CYS199 |
| D | ARG202 |
| D | CYS224 |
| D | LEU225 |
| D | CYS230 |
Functional Information from PROSITE/UniProt
| site_id | PS00507 |
| Number of Residues | 26 |
| Details | NI_HGENASE_L_1 Nickel-dependent hydrogenases large subunit signature 1. RGLEvilrgrdprdawafvERiCGVC |
| Chain | Residue | Details |
| A | ARG54-CYS79 |
| site_id | PS00508 |
| Number of Residues | 10 |
| Details | NI_HGENASE_L_2 Nickel-dependent hydrogenases large subunit signature 2. FDPCLACst.H |
| Chain | Residue | Details |
| A | PHE587-HIS596 |
