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Crystal structure of isoprenoid synthase A3MSH1 (target efi-501992) from pyrobaculum calidifontis complexed with dmapp

Analyse Crystal structure of isoprenoid synthase A3MSH1 (target efi-501992) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GP1
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polyprenyl synthetase
UniProt: A3MSH1
Ligands: DMA, CL
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polyprenyl synthetase	protein	331	76% helix, 2% strand	A3MSH1

Ligands and binding sites

DMA · Dimethylallyl diphosphate · ligand · chains A
CL · Chloride ion · ion · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	581	0.72	0.80	55	DMA

Compared structures

4GP1 · Crystal structure of ISOPRENOID SYNTHASE A3MSH1 (TARGET EFI-501992) from pyrobaculum… · 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 A3MSH1
Elsewhere: RCSB PDB 4GP1 · PDBe 4GP1 · UniProt A3MSH1

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