Research workbench
Crystal structure of 31KD heat shock protein, VCHSP31 from vibrio cholerae
Analyse Crystal structure of 31KD heat shock protein, VCHSP31 from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I2N
- Type
- protein
- Length
- 1,686 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intracellular PROTEASE/AMIDASE
- UniProt
- A5F0Q0
- Ligands
- CA
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Intracellular PROTEASE/AMIDASE | protein | 281 | 38% helix, 17% strand | A5F0Q0 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B, C, D, E, F
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A, B, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.75 | 0.84 | 68 | empty |
| 2 | 342 | 0.74 | 0.85 | 66 | empty |
| 3 | 885 | 0.72 | 0.77 | 79 | empty |
| 4 | 298 | 0.69 | 0.83 | 32 | empty |
| 5 | 185 | 0.67 | 0.86 | 40 | empty |
Interfaces
10 interfaces between chains.
- C–D · 1085 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1083 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 928 Ų buried · 18 hydrogen bonds · protein-protein
- C–F · 483 Ų buried · 7 hydrogen bonds · protein-protein
- B–F · 407 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4I2N · Crystal structure of 31kD Heat Shock Protein, VcHsp31 from Vibrio cholerae · 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 A5F0Q0
- Elsewhere: RCSB PDB 4I2N · PDBe 4I2N · UniProt A5F0Q0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.