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Esterase (eaest) from exiguobacterium antarcticum

Analyse Esterase (eaest) from exiguobacterium antarcticum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H3H
Type: protein
Length: 537 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Abhydrolase domain-containing protein
UniProt: K0ACL0
Ligands: F50
Pockets: 5 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Abhydrolase domain-containing protein	protein	268	45% helix, 18% strand	K0ACL0
B	Abhydrolase domain-containing protein	protein	269	45% helix, 19% strand	K0ACL0

Ligands and binding sites

F50 · Ethaneperoxoic acid · ligand · 2 copies · chains A, B

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

Pockets

5 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	214	0.53	0.78	29	empty
2	63	0.51	0.86	16	empty
3	56	0.45	0.84	14	empty
4	64	0.31	0.75	13	empty
5	55	0.25	0.72	13	empty

Interfaces

1 interface between chains.

A–B · 190 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5H3H · Esterase (EaEST) from Exiguobacterium antarcticum · 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 K0ACL0
Elsewhere: RCSB PDB 5H3H · PDBe 5H3H · UniProt K0ACL0

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