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Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis reveals the molecular basis of substrate specificity

Analyse Crystal structure of the acyltransferase domain of the iterative polyketide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AMP
Type: protein
Length: 372 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DYNE8
UniProt: Q84HI8
Ligands: CL
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DYNE8	protein	372	46% helix, 18% strand	Q84HI8

Ligands and binding sites

CL · Chloride ion · ion · chains A
MLI · Malonate ion · additive · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.63	0.81	35	MLI
2	95	0.35	0.74	19	empty
3	65	0.28	0.73	17	empty

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

4AMP · Crystal Structure of the Acyltransferase Domain of the Iterative Polyketide Synthase in… · 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 Q84HI8
Elsewhere: RCSB PDB 4AMP · PDBe 4AMP · UniProt Q84HI8

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