MolNFT v1 · #111248 · protein
Crystal structure of wild-type of HSP14.1 from sulfolobus solfatataricus P2
4YL9 · Heat shock protein HSP20: “Crystal structure of wild-type of HSP14.1 from sulfolobus solfatataricus P2”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.54). MolNFT v1 #111248 on GenesisL1: 3D structure, binding…
- PDB
- 4YL9
- Type
- protein
- Length
- 491 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP20
- UniProt
- D0KNS6
- Ligands
- CA
- Pockets
- 3 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Heat shock protein HSP20 | protein | 123 | 20% helix, 41% strand | D0KNS6 |
| C | Heat shock protein HSP20 | protein | 122 | 20% helix, 40% strand | D0KNS6 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains B, D
- EDO · 1,2-ethanediol · additive · 3 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.54 | 0.75 | 33 | empty |
| 2 | 90 | 0.31 | 0.73 | 21 | empty |
| 3 | 72 | 0.29 | 0.73 | 19 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1592 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 1539 Ų buried · 36 hydrogen bonds · protein-protein
- A–C · 226 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 61 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4YL9 · Crystal Structure of wild-type of hsp14.1 from Sulfolobus solfatataricus P2 · 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 D0KNS6
- Elsewhere: RCSB PDB 4YL9 · PDBe 4YL9 · UniProt D0KNS6
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