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The crystal structure of acyltransferase in complex with decanoyl-CoA and teicoplanin

Analyse The crystal structure of acyltransferase in complex with decanoyl-CoA and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q38
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein TCP24
EC: 2.3.1.-
UniProt: Q70AY4
Ligands: COA, TEC, SO4
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein TCP24 (EC 2.3.1.-)	protein	323	52% helix, 10% strand	Q70AY4

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
TEC · 2-amino-6-O-decanoyl-2-deoxy-beta-D-glucopyranose · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	642	0.71	0.79	66	COA, TEC
2	57	0.29	0.74	19	empty

Compared structures

4Q38 · The crystal structure of acyltransferase in complex with decanoyl-CoA and teicoplanin · 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 Q70AY4
Elsewhere: RCSB PDB 4Q38 · PDBe 4Q38 · UniProt Q70AY4

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