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Structure of a myristoyl-acp-specific thioesterase from vibrio harveyi

Analyse Structure of a myristoyl-acp-specific thioesterase from vibrio harveyi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1THT
Type: protein
Length: 587 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioesterase
UniProt: P05521
Pockets: 6 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioesterase	protein	294	41% helix, 20% strand	P05521
B	Thioesterase	protein	293	42% helix, 20% strand	P05521

Pockets

6 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	113	0.58	0.85	23	empty
2	165	0.54	0.80	33	empty
3	147	0.42	0.75	29	empty
4	80	0.32	0.74	21	empty
5	72	0.32	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 485 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1THT · Structure of a myristoyl-acp-specific thioesterase from vibrio harveyi · the same entry in another collection · chain A against A, TM-score 1.00
P05521 · AlphaFold monomer V2.0 prediction for acyl transferase (P05521) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P05521
Elsewhere: RCSB PDB 1THT · PDBe 1THT · UniProt P05521

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