Research workbench
Structure of eal enzyme BD1971 - apo form
Analyse Structure of eal enzyme BD1971 - apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQ2
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eal enzyme BD1971
- UniProt
- Q6MLN6
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eal enzyme BD1971 | protein | 108 | 27% helix, 40% strand | Q6MLN6 |
| B | Eal enzyme BD1971 | protein | 107 | 26% helix, 39% strand | Q6MLN6 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.49 | 0.77 | 24 | empty |
| 2 | 122 | 0.49 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1192 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6HQ2 · Structure of EAL Enzyme Bd1971 - apo form · 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 Q6MLN6
- Elsewhere: RCSB PDB 6HQ2 · PDBe 6HQ2 · UniProt Q6MLN6
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