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The crystal structure of a hemolysin domain from enterococcus faecalis V583
Analyse The crystal structure of a hemolysin domain from enterococcus faecalis V583 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R2Z
- Type
- protein
- Length
- 84 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolysin
- UniProt
- Q837X5
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin | protein | 84 | 20% helix, 40% strand | Q837X5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2R2Z · The crystal structure of a hemolysin domain from Enterococcus faecalis V583 · the same entry in another collection · 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 Q837X5
- Elsewhere: RCSB PDB 2R2Z · PDBe 2R2Z · UniProt Q837X5
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