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Orthorhombic structure of the acetyl esterase mekb

Analyse Orthorhombic structure of the acetyl esterase mekb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E4Y
Type: protein
Length: 693 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Homoserine O-acetyltransferase
EC: 2.3.1.-, 2.3.1.31
UniProt: Q0MRG5
Pockets: 11 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Homoserine O-acetyltransferase (EC 2.3.1.-, 2.3.1.31)	protein	347	44% helix, 16% strand	Q0MRG5
B	Homoserine O-acetyltransferase (EC 2.3.1.-, 2.3.1.31)	protein	346	43% helix, 16% strand	Q0MRG5

Pockets

11 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	79	0.74	0.97	16	empty
2	250	0.56	0.78	22	empty
3	120	0.45	0.78	20	empty
4	148	0.44	0.75	19	empty
5	113	0.44	0.78	20	empty

Interfaces

1 interface between chains.

A–B · 1309 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5E4Y · Orthorhombic structure of the acetyl esterase MekB · 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 Q0MRG5
Elsewhere: RCSB PDB 5E4Y · PDBe 5E4Y · UniProt Q0MRG5

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