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Bromide soaked structure of an esterase from the oil-degrading bacterium oleispira antarctica

Analyse Bromide soaked structure of an esterase from the oil-degrading bacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3S8Y
Type: protein
Length: 277 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase APC40077
EC: 3.1.1.2
UniProt: D0VWZ4
Ligands: BR
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase APC40077 (EC 3.1.1.2)	protein	277	39% helix, 25% strand	D0VWZ4

Ligands and binding sites

BR · Bromide ion · ion · chains A

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

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	73	0.33	0.74	14	BR

Compared structures

3S8Y · Bromide soaked structure of an esterase from the oil-degrading bacterium Oleispira… · 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 D0VWZ4
Elsewhere: RCSB PDB 3S8Y · PDBe 3S8Y · UniProt D0VWZ4

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