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Crystal structure of thermus thermophilus CSM6
Analyse Crystal structure of thermus thermophilus CSM6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FSH
- Type
- protein
- Length
- 907 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSM6
- UniProt
- Q53W17
- Ligands
- NI
- Pockets
- 12 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSM6 | protein | 459 | 61% helix, 8% strand | Q53W17 |
| B | CSM6 | protein | 448 | 61% helix, 8% strand | Q53W17 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 737 | 0.71 | 0.77 | 45 | empty |
| 2 | 497 | 0.62 | 0.75 | 48 | empty |
| 3 | 382 | 0.61 | 0.77 | 33 | empty |
| 4 | 189 | 0.52 | 0.78 | 31 | empty |
| 5 | 204 | 0.49 | 0.76 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 3009 Ų buried · 18 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 Q53W17
- Elsewhere: RCSB PDB 5FSH · PDBe 5FSH · UniProt Q53W17
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