Research workbench
[fefe]-hydrogenase maturase hyde from T. maritima (C-ter stretch absent)
Analyse [fefe]-hydrogenase maturase hyde from T. maritima (C-ter stretch absent) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O1P
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- [fefe] hydrogenase maturase subunit hyde
- EC
- 1.8.-.-
- UniProt
- Q9X0Z6
- Ligands
- CPS, SF4, SAH, CL, CO3
- Pockets
- 1 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | [fefe] hydrogenase maturase subunit hyde (EC 1.8.-.-) | protein | 332 | 45% helix, 13% strand | Q9X0Z6 |
Ligands and binding sites
- CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 5 copies · chains A
- SF4 · Iron/sulfur cluster · ligand · chains A
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- CO3 · Carbonate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 573 | 0.87 | 0.92 | 76 | SF4, SAH, CL |
Compared structures
- 7O1P · [FeFe]-hydrogenase maturase HydE from T. Maritima (C-ter stretch absent) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0Z6 · AlphaFold monomer V2.0 prediction for [fefe] hydrogenase maturase subunit hyde (Q9X0Z6) · a predicted model of the same protein · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9X0Z6
- Elsewhere: RCSB PDB 7O1P · PDBe 7O1P · UniProt Q9X0Z6
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