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Crystal structure of the brevianamide F prenyltransferase FTMPT1 from aspergillus fumigatus

Analyse Crystal structure of the brevianamide F prenyltransferase FTMPT1 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3O24
Type: protein
Length: 430 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Brevianamide F prenyltransferase
UniProt: Q4G2I1
Ligands: CL, SO4
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Brevianamide F prenyltransferase	protein	430	40% helix, 20% strand	Q4G2I1

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A
SO4 · Sulfate ion · ion · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	373	0.77	0.87	51	empty
2	251	0.63	0.82	31	SO4
3	105	0.39	0.76	28	empty
4	50	0.24	0.72	11	empty

Compared structures

3O24 · Crystal structure of the brevianamide F prenyltransferase FtmPT1 from Aspergillus… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q4G2I1
Elsewhere: RCSB PDB 3O24 · PDBe 3O24 · UniProt Q4G2I1

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