MolNFT v1 · #103947 · protein
ALPHA/BETA hydrolase fold protein from chitinophaga pinensis
4PW0: “ALPHA/BETA hydrolase fold protein from chitinophaga pinensis”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.57). MolNFT v1 #103947 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4PW0
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA hydrolase fold protein
- UniProt
- C7PEX8
- Ligands
- CL
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA/BETA hydrolase fold protein | protein | 275 | 45% helix, 17% strand | C7PEX8 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A
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 | 269 | 0.57 | 0.77 | 30 | CL |
| 2 | 55 | 0.34 | 0.78 | 15 | empty |
| 3 | 54 | 0.33 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4PW0 · Alpha/beta hydrolase fold protein from Chitinophaga pinensis · 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 C7PEX8
- Elsewhere: RCSB PDB 4PW0 · PDBe 4PW0 · UniProt C7PEX8
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