Research workbench
Crystal structure of besa (P21 form)
Analyse Crystal structure of besa (P21 form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KKT
- Type
- protein
- Length
- 1,052 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane fusion protein
- UniProt
- O51166
- Pockets
- 16 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane fusion protein | protein | 265 | 6% helix, 59% strand | O51166 |
| B | Membrane fusion protein | protein | 262 | 6% helix, 58% strand | O51166 |
| C | Membrane fusion protein | protein | 262 | 7% helix, 59% strand | O51166 |
| D | Membrane fusion protein | protein | 263 | 7% helix, 58% strand | O51166 |
Pockets
16 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.67 | 0.80 | 35 | empty |
| 2 | 352 | 0.65 | 0.80 | 32 | empty |
| 3 | 127 | 0.46 | 0.78 | 19 | empty |
| 4 | 115 | 0.44 | 0.77 | 20 | empty |
| 5 | 92 | 0.41 | 0.77 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1102 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1001 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 941 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 934 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 48 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4KKT · Crystal Structure of BesA (P21 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 O51166
- Elsewhere: RCSB PDB 4KKT · PDBe 4KKT · UniProt O51166
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