Research workbench
Structure of thermus thermophilus casa (CSE1)
Analyse Structure of thermus thermophilus casa (CSE1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AN8
- Type
- protein
- Length
- 919 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSE1
- UniProt
- Q53VY1
- Pockets
- 10 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSE1 | protein | 468 | 46% helix, 19% strand | Q53VY1 |
| B | CSE1 | protein | 451 | 45% helix, 19% strand | Q53VY1 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.54 | 0.81 | 24 | ACT |
| 2 | 214 | 0.54 | 0.78 | 25 | empty |
| 3 | 245 | 0.54 | 0.76 | 24 | empty |
| 4 | 369 | 0.53 | 0.73 | 43 | empty |
| 5 | 98 | 0.53 | 0.83 | 22 | ACT |
Interfaces
1 interface between chains.
- A–B · 278 Ų buried · 0 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 Q53VY1
- Elsewhere: RCSB PDB 4AN8 · PDBe 4AN8 · UniProt Q53VY1
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