MolNFT v1 · #91596 · protein
Crystal structure of a carboxyl esterase at 2.0 ångström resolution
4FHZ · PHOSPHOLIPASE/CARBOXYLESTERASE: “Crystal structure of a carboxyl esterase at 2.0 ångström resolution”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.45). MolNFT v1 #91596 on GenesisL1: 3D structure, binding sites…
- PDB
- 4FHZ
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PHOSPHOLIPASE/CARBOXYLESTERASE
- EC
- 3.1.1.1
- UniProt
- Q3J2V1
- Ligands
- NA
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PHOSPHOLIPASE/CARBOXYLESTERASE (EC 3.1.1.1) | protein | 220 | 41% helix, 20% strand | Q3J2V1 |
Ligands and binding sites
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 | 130 | 0.45 | 0.76 | 25 | PEG, NA |
Compared structures
- 4FHZ · Crystal structure of a carboxyl esterase at 2.0 angstrom resolution · 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 Q3J2V1
- Elsewhere: RCSB PDB 4FHZ · PDBe 4FHZ · UniProt Q3J2V1
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