Research workbench
Hybrid cluster protein (hcp) from escherichia COLI
Analyse Hybrid cluster protein (hcp) from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DE4
- Type
- protein
- Length
- 550 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxylamine reductase
- EC
- 1.7.99.1
- UniProt
- P75825
- Ligands
- SF4, FS2
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxylamine reductase (EC 1.7.99.1) | protein | 550 | 45% helix, 11% strand | P75825 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.76 | 0.98 | 22 | empty |
| 2 | 152 | 0.69 | 0.88 | 44 | empty |
| 3 | 66 | 0.66 | 0.93 | 22 | empty |
| 4 | 53 | 0.50 | 0.87 | 17 | empty |
| 5 | 87 | 0.43 | 0.79 | 18 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
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 P75825
- Elsewhere: RCSB PDB 7DE4 · PDBe 7DE4 · UniProt P75825
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