MolNFT v1 · #85779 · protein

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

4AMP · DYNE8: “Crystal structure of the acyltransferase domain of the iterative polyketide synthase in enediyne biosynthesis…”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.63). MolNFT v1 #85779 on GenesisL1: 3D…

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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