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Esterase LPEST1 from lactobacillus plantarum: native structure

Analyse Esterase LPEST1 from lactobacillus plantarum: native structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C88
Type: protein
Length: 1,352 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
UniProt: Q88Y25
Pockets: 8 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Esterase (EC 3.1.1.1)	protein	338	37% helix, 20% strand	Q88Y25
B	Esterase (EC 3.1.1.1)	protein	337	37% helix, 21% strand	Q88Y25
C	Esterase (EC 3.1.1.1)	protein	339	37% helix, 20% strand	Q88Y25

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1005	0.78	0.80	78	empty
2	437	0.69	0.80	38	empty
3	415	0.67	0.79	39	empty
4	414	0.66	0.79	39	empty
5	259	0.66	0.83	35	empty

Interfaces

3 interfaces between chains.

B–D · 1142 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 965 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 475 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4C88 · Esterase LpEst1 from Lactobacillus plantarum: native structure · 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 Q88Y25
Elsewhere: RCSB PDB 4C88 · PDBe 4C88 · UniProt Q88Y25

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