MolNFT v1 · #121464 · protein

The structural and biochemical characterization of acyl-CoA hydrolase mutant ASN28ALA from staphylococcus aureus.

5HWF · Thioesterase: “The structural and biochemical characterization of acyl-CoA hydrolase mutant ASN28ALA from staphylococcus…”. X-ray diffraction, 1 pocket (best druggability 0.31). MolNFT v1 #121464 on GenesisL1: 3D structure, binding…

PDB: 5HWF
Type: protein
Length: 167 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioesterase
UniProt: A0A0H3K033
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioesterase	protein	167	35% helix, 40% strand	A0A0H3K033

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.31	0.77	14	empty

Compared structures

5HWF · The structural and biochemical characterization of acyl-coa hydrolase mutant Asn28Ala… · the same entry in another collection · chain A against A, TM-score 1.00

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 A0A0H3K033
Elsewhere: RCSB PDB 5HWF · PDBe 5HWF · UniProt A0A0H3K033

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