Research workbench

Plant carboxylesterase AECXE1 from actinidia eriantha with acyl adduct

Analyse Plant carboxylesterase AECXE1 from actinidia eriantha with acyl adduct in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O7R
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cxe carboxylesterase
EC: 3.1.1.1
UniProt: Q0ZPV7
Ligands: 4PA
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cxe carboxylesterase (EC 3.1.1.1)	protein	307	37% helix, 22% strand	Q0ZPV7

Ligands and binding sites

4PA · Propyl acetate · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	266	0.66	0.82	36	4PA
2	64	0.52	0.86	17	empty
3	93	0.32	0.73	19	empty
4	57	0.27	0.73	15	empty

Compared structures

2O7R · Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct · the same entry in another collection · chain A against A, TM-score 1.00
Q0ZPV7 · AlphaFold monomer V2.0 prediction for carboxylesterase 1 (Q0ZPV7) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q0ZPV7
Elsewhere: RCSB PDB 2O7R · PDBe 2O7R · UniProt Q0ZPV7

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