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The structure of a novel thermophilic esterase from the planctomycetes species, thermogutta terrifontis, EST2-propionate bound

Analyse The structure of a novel thermophilic esterase from the planctomycetes species… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AOA
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
EC: 3.1.1.1
Ligands: CL
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase (EC 3.1.1.1)	protein	272	37% helix, 21% strand	—

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
PG4 · Tetraethylene glycol · additive · 2 copies · chains A
PPI · Propanoic acid · additive · 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	134	0.40	0.74	23	PEG, EDO

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

5AOA · The structure of a novel thermophilic esterase from the Planctomycetes species… · 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
Elsewhere: RCSB PDB 5AOA · PDBe 5AOA

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