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Crystal structure of an acyl-acp thioesterase (NP_810988.1) from bacteroides thetaiotaomicron vpi-5482 at 1.90 a resolution

Analyse Crystal structure of an acyl-acp thioesterase (NP_810988.1) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ESS
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acyl-acp thioesterase
UniProt: Q8A611
Ligands: CA, CL
Pockets: 3 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acyl-acp thioesterase	protein	243	21% helix, 42% strand	Q8A611

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A

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

Pockets

3 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	318	0.59	0.77	38	CA, MPD
2	180	0.56	0.80	22	empty
3	102	0.43	0.78	18	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2ESS · Crystal structure of an acyl-ACP thioesterase (NP_810988.1) from Bacteroides… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q8A611
Elsewhere: RCSB PDB 2ESS · PDBe 2ESS · UniProt Q8A611

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