Research workbench
Comparison of the structure and activity of glycosylated and aglycosylated human carboxylesterase 1
Analyse Comparison of the structure and activity of glycosylated and aglycosylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A7G
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Liver carboxylesterase 1
- EC
- 3.1.1.1, 3.1.1.56
- UniProt
- P23141
- Ligands
- NAG
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Liver carboxylesterase 1 (EC 3.1.1.1, 3.1.1.56) | protein | 529 | 38% helix, 17% strand | P23141 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.80 | 0.90 | 43 | empty |
| 2 | 410 | 0.68 | 0.80 | 57 | empty |
| 3 | 105 | 0.38 | 0.75 | 29 | empty |
| 4 | 78 | 0.35 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5A7G · Comparison of the structure and activity of glycosylated and aglycosylated Human… · the same entry in another collection · chain A against A, TM-score 1.00
- P23141 · AlphaFold monomer V2.0 prediction for liver carboxylesterase 1 (P23141) · a predicted model of the same protein · 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 P23141
- Elsewhere: RCSB PDB 5A7G · PDBe 5A7G · UniProt P23141
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