Research workbench
Complete crystal structure of carboxylesterase cest-2923 (LP_2923) from lactobacillus plantarum WCFS1
Analyse Complete crystal structure of carboxylesterase cest-2923 (LP_2923) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C01
- Type
- protein
- Length
- 1,650 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cest-2923
- EC
- 3.1.1.1
- UniProt
- F9US10
- Ligands
- CCN, QY9, SO4
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Cest-2923 (EC 3.1.1.1) | protein | 275 | 33% helix, 20% strand | F9US10 |
Ligands and binding sites
- CCN · Acetonitrile · ligand · 12 copies · chains A, D, B, C, E, F
- QY9 · phenyl acetate · ligand · 5 copies · chains A, E, B, C, F, D
- SO4 · Sulfate ion · ion · 8 copies · chains A, B, E, C, F, D
- ACT · Acetate ion · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.87 | 0.89 | 121 | CCN, QY9 |
| 2 | 1054 | 0.86 | 0.88 | 128 | QY9, CCN |
| 3 | 491 | 0.81 | 0.88 | 58 | QY9 |
| 4 | 411 | 0.80 | 0.89 | 60 | QY9, CCN |
| 5 | 369 | 0.68 | 0.81 | 37 | empty |
Interfaces
12 interfaces between chains.
- B–E · 1565 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 1528 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1523 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 474 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 473 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4C01 · Complete crystal structure of carboxylesterase Cest-2923 (lp_2923) from Lactobacillus… · 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 F9US10
- Elsewhere: RCSB PDB 4C01 · PDBe 4C01 · UniProt F9US10
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.