MolNFT v1 · #74638 · protein

Crystal structure of the fluoroacetyl-CoA-specific thioesterase flk in an open conformation

3P2S · Fluoroacetyl coenzyme a thioesterase: “Crystal structure of the fluoroacetyl-CoA-specific thioesterase flk in an open conformation”. X-ray diffraction, 3 pockets (best druggability 0.65). MolNFT v1 #74638 on GenesisL1: 3D structure…

PDB: 3P2S
Type: protein
Length: 266 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluoroacetyl coenzyme a thioesterase
UniProt: Q1EMV2
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fluoroacetyl coenzyme a thioesterase	protein	133	31% helix, 41% strand	Q1EMV2

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	94	0.65	0.90	25	empty
2	198	0.64	0.83	42	empty
3	91	0.46	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 2053 Å² buried · 30 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3P2S · Crystal structure of the fluoroacetyl-CoA-specific thioesterase FlK in an open… · the same entry in another collection · chain A against A, TM-score 1.00
Q1EMV2 · AlphaFold monomer V2.0 prediction for fluoroacetyl-CoA thioesterase (Q1EMV2) · 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 Q1EMV2
Elsewhere: RCSB PDB 3P2S · PDBe 3P2S · UniProt Q1EMV2

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