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Crystal structure of the E.COLI thioesterase II, a homologue of the human nef-binding enzyme

Analyse Crystal structure of the E.COLI thioesterase II, a homologue of the human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C8U
Type: protein
Length: 570 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-CoA thioesterase II
EC: 3.1.2.-
UniProt: P23911
Pockets: 5 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acyl-CoA thioesterase II (EC 3.1.2.-)	protein	285	19% helix, 39% strand	P23911

Ligands and binding sites

LDA · Lauryl dimethylamine-N-oxide · additive · 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	973	0.78	0.80	76	LDA
2	913	0.77	0.80	74	LDA
3	62	0.48	0.84	16	empty
4	62	0.46	0.83	15	empty
5	100	0.36	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 2596 Å² buried · 57 hydrogen bonds · protein-protein

Compared structures

1C8U · Crystal structure of the E.COLI thioesterase II, a homologue of the human nef-binding… · 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 P23911
Elsewhere: RCSB PDB 1C8U · PDBe 1C8U · UniProt P23911

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