Research workbench
Crystal structure of CheC-like superfamily protein (YP_001095400.1) from Shewanella SP. PV-4 at 2.13 A resolution
Analyse Crystal structure of CheC-like superfamily protein (YP_001095400.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IIC
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.13
- Source
- Shewanella loihica PV-4
- Molecule
- CheC domain protein
- UniProt
- A3QI43
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · resolution 2.13 · 1 distinct chain · 36% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | CheC domain protein | protein | 154 | 36% helix, 34% strand | A3QI43 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.31 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 3IIC · Crystal structure of chec-like superfamily protein (YP_001095400.1) from shewanella sp.… · 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 A3QI43
- Elsewhere: RCSB PDB 3IIC · PDBe 3IIC · UniProt A3QI43
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