5JSH
The 3D structure of recombinant [NiFeSe] hydrogenase from Desulfovibrio Vulgaris Hildenborough in the oxidized state at 1.30 Angstrom
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 | 8 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | HIS208 |
| A | CYS211 |
| A | TYR213 |
| A | LEU214 |
| A | CYS232 |
| A | ARG233 |
| A | CYS238 |
| A | VAL260 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SF4 A 302 |
| Chain | Residue |
| A | CYS247 |
| A | TRP252 |
| A | CYS259 |
| A | CYS265 |
| A | ILE266 |
| A | CYS268 |
| B | ARG182 |
| B | GLN187 |
| A | THR243 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue SF4 A 303 |
| Chain | Residue |
| A | GLY17 |
| A | CYS18 |
| A | CYS21 |
| A | GLU77 |
| A | GLY119 |
| A | THR120 |
| A | CYS121 |
| A | GLY158 |
| A | CYS159 |
| A | PRO160 |
| A | 6ML304 |
| B | ARG73 |
| B | HIS185 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 6ML A 304 |
| Chain | Residue |
| A | CYS18 |
| A | THR19 |
| A | GLY20 |
| A | CYS21 |
| A | GLU77 |
| A | GLY78 |
| A | THR120 |
| A | CYS121 |
| A | GLY158 |
| A | CYS159 |
| A | PRO160 |
| A | SF4303 |
| A | HOH444 |
| B | HIS185 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue FCO B 601 |
| Chain | Residue |
| B | CYS78 |
| B | ALA420 |
| B | PRO421 |
| B | ARG422 |
| B | LEU425 |
| B | ALA444 |
| B | SER445 |
| B | SEC489 |
| B | CYS492 |
| B | NI602 |
| B | H2S604 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NI B 602 |
| Chain | Residue |
| B | CSD75 |
| B | CYS78 |
| B | SEC489 |
| B | CYS492 |
| B | FCO601 |
| B | H2S604 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue FE2 B 603 |
| Chain | Residue |
| B | GLU56 |
| B | ILE441 |
| B | HIS495 |
| B | HOH723 |
| B | HOH730 |
| B | HOH753 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue H2S B 604 |
| Chain | Residue |
| B | CSD75 |
| B | CYS78 |
| B | ARG422 |
| B | SEC489 |
| B | FCO601 |
| B | NI602 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 605 |
| Chain | Residue |
| B | CYS78 |
| B | THR80 |
| B | ALA81 |
| B | PHE110 |
| B | ASN113 |
| B | PRO421 |
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 |
