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Crystal structure of the exsa regulatory domain
Analyse Crystal structure of the exsa regulatory domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZUA
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exoenzyme S synthesis regulatory protein exsa
- UniProt
- P26993
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exoenzyme S synthesis regulatory protein exsa | protein | 155 | 36% helix, 30% strand | P26993 |
| B | Exoenzyme S synthesis regulatory protein exsa | protein | 151 | 32% helix, 31% strand | P26993 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.59 | 0.79 | 36 | empty |
| 2 | 197 | 0.56 | 0.79 | 25 | empty |
| 3 | 88 | 0.41 | 0.77 | 16 | empty |
| 4 | 111 | 0.36 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 509 Ų buried · 1 hydrogen bond · 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 P26993
- Elsewhere: RCSB PDB 4ZUA · PDBe 4ZUA · UniProt P26993
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