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Ferulic acid esterase from Streptomyces cinnamoneus at 1.5 A resolution

Analyse Ferulic acid esterase from Streptomyces cinnamoneus at 1.5 A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YAL
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: Streptomyces cinnamoneus
Molecule: Esterase
EC: 3.1.1.73
UniProt: A0A0M4UW33
Ligands: NA
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.73)	protein	342	36% helix, 24% strand	A0A0M4UW33

Ligands and binding sites

NA · Sodium ion · metal · chains A
ACT · Acetate ion · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	160	0.54	0.80	21	empty
2	144	0.49	0.78	19	empty
3	92	0.34	0.74	21	NA

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5YAL · Ferulic acid esterase from streptomyces cinnamoneus at 1.5 a resolution · 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 A0A0M4UW33
Elsewhere: RCSB PDB 5YAL · PDBe 5YAL · UniProt A0A0M4UW33

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