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Crystal structure of the C-terminal domain of ypbh
Analyse Crystal structure of the C-terminal domain of ypbh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JTO
- Type
- protein
- Length
- 550 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adapter protein meca 2
- UniProt
- P50734
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 5 distinct chains · 42% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Adapter protein meca 2 | protein | 94 | 43% helix, 31% strand | P50734 |
| B | Adapter protein meca 2 | protein | 90 | 43% helix, 24% strand | P50734 |
| C | Adapter protein meca 2 | protein | 92 | 45% helix, 32% strand | P50734 |
| E | Adapter protein meca 2 | protein | 89 | 40% helix, 24% strand | P50734 |
| F | Adapter protein meca 2 | protein | 91 | 40% helix, 24% strand | P50734 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.58 | 0.85 | 18 | empty |
| 2 | 200 | 0.57 | 0.80 | 30 | empty |
| 3 | 229 | 0.55 | 0.78 | 41 | empty |
| 4 | 253 | 0.49 | 0.74 | 33 | empty |
| 5 | 113 | 0.34 | 0.72 | 24 | empty |
Interfaces
8 interfaces between chains.
- C–D · 549 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 541 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 531 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 432 Ų buried · 11 hydrogen bonds · protein-protein
- D–F · 337 Ų buried · 4 hydrogen bonds · protein-protein
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 P50734
- Elsewhere: RCSB PDB 3JTO · PDBe 3JTO · UniProt P50734
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