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Crystal structure of MYCELIOPHTERIA_THERMOPHILA CPS50 (SWD1) beta- propeller domain
Analyse Crystal structure of MYCELIOPHTERIA_THERMOPHILA CPS50 (SWD1) beta- propeller… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E29
- Type
- protein
- Length
- 1,268 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SWD1-like protein
- UniProt
- G2Q1Q9
- Pockets
- 13 · best druggability 0.89
Structure
x-ray diffraction · 4 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | SWD1-like protein | protein | 312 | 1% helix, 53% strand | G2Q1Q9 |
| A | SWD1-like protein | protein | 327 | 3% helix, 50% strand | G2Q1Q9 |
| B | SWD1-like protein | protein | 315 | 3% helix, 52% strand | G2Q1Q9 |
| C | SWD1-like protein | protein | 314 | 1% helix, 53% strand | G2Q1Q9 |
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1031 | 0.89 | 0.91 | 110 | empty |
| 2 | 961 | 0.78 | 0.80 | 95 | empty |
| 3 | 336 | 0.76 | 0.87 | 39 | empty |
| 4 | 350 | 0.74 | 0.85 | 35 | empty |
| 5 | 389 | 0.69 | 0.81 | 45 | empty |
Interfaces
4 interfaces between chains.
- D–A · 1248 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 646 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 364 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 79 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6E29 · Crystal structure of Myceliophteria_thermophila Cps50 (Swd1) beta-propeller domain · the same entry in another collection · chain D against D, 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 G2Q1Q9
- Elsewhere: RCSB PDB 6E29 · PDBe 6E29 · UniProt G2Q1Q9
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