UniProt P29166
Iron hydrogenase 1 (P29166)
Iron hydrogenase 1 (UniProt P29166), EC 1.12.7.2: 46 experimental structures on GenesisL1, 11 ligands bound, 141 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P29166
- Protein
- Iron hydrogenase 1
- EC
- 1.12.7.2
- Experimental structures
- 46
- Predicted models
- 0
- Ligands
- 11
- Pockets
- 141 · 9 records with a druggable one
Structures
46 records of P29166 in the MolNFT archive: 46 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1C4A | Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi)… | x-ray diffraction | A | — | — |
| 1C4A | Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi)… | x-ray diffraction | A | — | — |
| 1C4C | Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi)… | x-ray diffraction | A | — | — |
| 1C4C | Binding of exogenously added carbon monoxide at the active site of the fe-only hydrogenase (cpi)… | x-ray diffraction | A | — | — |
| 1FEH | Fe-only hydrogenase from clostridium pasteurianum | x-ray diffraction | A | — | — |
| 1FEH | Fe-only hydrogenase from clostridium pasteurianum | x-ray diffraction | A | — | — |
| 3C8Y | 1.39 Angstrom crystal structure of Fe-only hydrogenase | x-ray diffraction | A | — | — |
| 3C8Y | 1.39 ångström crystal structure of fe-only hydrogenase | x-ray diffraction | A | — | — |
| 4XDC | Active semisynthetic [FeFe]-hydrogenase CpI with aza-dithiolato-bridged [2Fe] cofactor | x-ray diffraction | A, B | — | — |
| 4XDC | Active semisynthetic [fefe]-hydrogenase cpi with aza-dithiolato- bridged [2FE] cofactor | x-ray diffraction | A, B | — | — |
| 4XDD | Apo [FeFe]-Hydrogenase CpI | x-ray diffraction | A, B | — | — |
| 4XDD | Apo [fefe]-hydrogenase cpi | x-ray diffraction | A, B | — | — |
| 5BYQ | Semisynthetic [FeFe]-hydrogenase CpI with oxodithiolato-bridged [2Fe] cofactor | x-ray diffraction | A, B | — | — |
| 5BYQ | Semisynthetic [fefe]-hydrogenase cpi with oxodithiolato-bridged [2FE] cofactor | x-ray diffraction | A, B | — | — |
| 5BYR | Semisynthetic [FeFe]-hydrogenase CpI with propane-dithiolato-bridged [2Fe] cofactor | x-ray diffraction | A, B | — | — |
| 5BYR | Semisynthetic [fefe]-hydrogenase cpi with propane-dithiolato-bridged [2FE] cofactor | x-ray diffraction | A, B | — | — |
| 5BYS | Semisynthetic [fefe]-hydrogenase cpi with sulfur-dithiolato-bridged [2FE] cofactor | x-ray diffraction | A, B | — | — |
| 5LA3 | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E279A | x-ray diffraction | A, B | 402, SF4, FES, MG | 16 (best 0.80) |
| 5LA3 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant E279A | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 5OEF | Active semisynthetic [fefe]-hydrogenase cpi with aza-diselenato- bridged [2FE] cofactor | x-ray diffraction | A, B | 9SQ, SF4, FES, MG | — |
| 6GLY | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant C299A | x-ray diffraction | A, B | 402, SF4, FES, MG | 16 (best 0.80) |
| 6GLY | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant C299A | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GLZ | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant C299D | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM0 | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E279Q | x-ray diffraction | A, B | 402, SF4, FES, MG | 17 (best 0.79) |
| 6GM0 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant E279Q | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM1 | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E282A | x-ray diffraction | A, B | 402, SF4, FES, MG | 18 (best 0.81) |
| 6GM1 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant E282A | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM2 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant E282D | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM3 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant R286A | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM4 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant S319A | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM8 | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E282Q | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6GM8 | [fefe]-hydrogenase cpi from clostridium pasteurianum, variant E282Q | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 6H63 | Semisynthetic [FeFe]-hydrogenase CpI with ethanedithiolate [2Fe] cofactor | x-ray diffraction | A, B | FU8, SF4, FES, MG | — |
| 6H63 | Semisynthetic [fefe]-hydrogenase cpi with ethanedithiolate [2FE] cofactor | x-ray diffraction | A, B | FU8, SF4, FES, MG | — |
| 6N59 | 1.0 Angstrom crystal structure of [FeFe]-hydrogenase | x-ray diffraction | A | 402, SF4, FES | 7 (best 0.80) |
| 6N59 | 1.0 ångström crystal structure of [fefe]-hydrogenase | x-ray diffraction | A | 402, SF4, FES | — |
| 6N6P | Crystal structure of [FeFe]-hydrogenase in the presence of 7 mM Sodium dithionite | x-ray diffraction | A | 402, SF4, FES | — |
| 6N6P | Crystal structure of [fefe]-hydrogenase in the presence of 7 mm sodium dithionite | x-ray diffraction | A | 402, SF4, FES | — |
| 6NAC | Crystal structure of [fefe]-hydrogenase I (cpi) solved with single pulse free electron laser data | x-ray diffraction | A | 402, SF4, FES | — |
| 6YF4 | [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI), variant E279D | x-ray diffraction | A, B | 402, SF4, FES, MG | 16 (best 0.80) |
| 6YF4 | [fefe]-hydrogenase I from clostridium pasteurianum (cpi), variant E279D | x-ray diffraction | A, B | 402, SF4, FES, MG | — |
| 8ALN | CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.34 Angstrom | x-ray diffraction | A, B | SF4, FES, MG, MHX, CL | — |
| 8AP2 | cyanide-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI) at 1.39 Angstrom | x-ray diffraction | A, B | SF4, FES, CL, MG, VHR | 20 (best 0.80) |
| 8CJY | [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant S357T | x-ray diffraction | A, B | 402, SF4, FES, MG, CL | 15 (best 0.80) |
| 8PVM | formaldehyde-inhibited [FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant C299D | x-ray diffraction | A, B | 402, SF4, FES, 74C, FOR, MG | 16 (best 0.80) |
| P29166 | AlphaFold monomer V2.0 prediction for iron hydrogenase 1 (P29166) | — | — | — |
Ligands
- FES · Fe2/s2 (inorganic) cluster · in 28 records
- SF4 · Iron/sulfur cluster · in 28 records
- 402 · dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+) · in 23 records
- MG · Magnesium ion · in 23 records
- CL · Chloride ion · in 4 records
- FU8 · dicarbonyl[bis(cyanide-kappaC)]-mu-(ethanethiolatato-1kappaS:2kappaS)-mu-(ox omethylidene)diiron(2+) · in 2 records
- 74C · methyl radical · in 1 record
- 9SQ · Dicarbonyl[bis(cyanide-kappac)]-mu-(iminodimethaneselenato- 1kappas:2kappas)-mu-(oxomethylidene)diiron(2+) · in 1 record
- FOR · Formyl group · in 1 record
- MHX · Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CO form) · in 1 record
- VHR · Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CN form) · in 1 record
Elsewhere
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