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Crystal structure of acetyl ester-xyloside bifunctional hydrolase from caldicellulosiruptor lactoaceticus

Analyse Crystal structure of acetyl ester-xyloside bifunctional hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A6O
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ESTERASE/LIPASE-like protein
UniProt: G2PVG6
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ESTERASE/LIPASE-like protein	protein	272	33% helix, 18% strand	G2PVG6

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.33	0.77	17	empty

Compared structures

6A6O · Crystal structure of acetyl ester-xyloside bifunctional hydrolase from… · 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 G2PVG6
Elsewhere: RCSB PDB 6A6O · PDBe 6A6O · UniProt G2PVG6

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