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Crystal Structure of DphMB1
Analyse Crystal Structure of DphMB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K34
- Type
- protein
- Length
- 1,204 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Mycobacterium sp. YC-RL4
- Molecule
- Lipase
- UniProt
- A0A172UPQ1
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.5 · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D | Lipase | protein | 301 | 40% helix, 16% strand | A0A172UPQ1 |
Pockets
15 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.78 | 0.85 | 97 | empty |
| 2 | 306 | 0.78 | 0.89 | 60 | empty |
| 3 | 241 | 0.76 | 0.89 | 38 | empty |
| 4 | 246 | 0.73 | 0.87 | 37 | empty |
| 5 | 224 | 0.72 | 0.87 | 37 | empty |
Interfaces
3 interfaces between chains.
- C–D · 724 Ų buried · 8 hydrogen bonds · protein-protein
- B–A · 721 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 502 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6K34 · Crystal structure of DPHMB1 · 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 A0A172UPQ1
- Elsewhere: RCSB PDB 6K34 · PDBe 6K34 · UniProt A0A172UPQ1
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