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Trigonal crystal structure of an acetylester hydrolase from corynebacterium glutamicum

Analyse Trigonal crystal structure of an acetylester hydrolase from corynebacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5D7B
Type: protein
Length: 698 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: Q8NS43
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Homoserine O-acetyltransferase (EC 2.3.1.-, 2.3.1.31)	protein	349	45% helix, 15% strand	Q8NS43

Ligands and binding sites

GOL · Glycerol · additive · 15 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	168	0.63	0.84	31	GOL
2	159	0.61	0.83	26	GOL
3	180	0.55	0.80	18	empty
4	78	0.45	0.81	18	empty
5	64	0.43	0.82	19	empty

Interfaces

1 interface between chains.

A–B · 1450 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5D7B · Trigonal Crystal Structure of an acetylester hydrolase from Corynebacterium glutamicum · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8NS43
Elsewhere: RCSB PDB 5D7B · PDBe 5D7B · UniProt Q8NS43

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