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Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone sura from salmonella enterica subsp. enterica serovar typhimurium str. 14028S
Analyse Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G2P
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone sura
- UniProt
- D0ZJR9
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chaperone sura | protein | 108 | 35% helix, 29% strand | D0ZJR9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.53 | 0.77 | 30 | empty |
| 2 | 52 | 0.32 | 0.77 | 14 | GOL |
Interfaces
1 interface between chains.
- A–B · 230 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 4G2P · Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone… · the same entry in another collection · chain B against B, 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 D0ZJR9
- Elsewhere: RCSB PDB 4G2P · PDBe 4G2P · UniProt D0ZJR9
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