Research workbench
Crystal structure of the bid domain of BEP9 from bartonella clarridgeiae
Analyse Crystal structure of the bid domain of BEP9 from bartonella clarridgeiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YK2
- Type
- protein
- Length
- 213 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bartonella effector protein (bep) substrate of virb T4SS
- UniProt
- E6YIM5
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bartonella effector protein (bep) substrate of virb T4SS | protein | 107 | 74% helix, 4% strand | E6YIM5 |
| B | Bartonella effector protein (bep) substrate of virb T4SS | protein | 106 | 75% helix, 4% strand | E6YIM5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 607 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4YK2 · Crystal Structure of the BID Domain of Bep9 from Bartonella clarridgeiae · 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 E6YIM5
- Elsewhere: RCSB PDB 4YK2 · PDBe 4YK2 · UniProt E6YIM5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.