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Crystal structure of a cloned feruloyl esterase from a soil metagenomic library

Analyse Crystal structure of a cloned feruloyl esterase from a soil metagenomic library in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZRS
Type: protein
Length: 584 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
UniProt: E7DJY5
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Esterase	protein	292	42% helix, 17% strand	E7DJY5

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 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	761	0.78	0.82	55	empty
2	140	0.52	0.79	19	empty
3	133	0.50	0.79	19	empty
4	86	0.48	0.82	18	empty
5	177	0.47	0.76	22	GOL

Interfaces

1 interface between chains.

A–B · 1062 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 disulfide (nonstandard, disulfide).

Compared structures

4ZRS · Crystal structure of a cloned feruloyl esterase from a soil metagenomic library · 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 E7DJY5
Elsewhere: RCSB PDB 4ZRS · PDBe 4ZRS · UniProt E7DJY5

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