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The crystal structure of a radical SAM enzyme blse involved in the biosynthesis of blasticidin S

Analyse The crystal structure of a radical SAM enzyme blse involved in the biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7VOB
Type: protein
Length: 327 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosylglucuronate decarboxylase
UniProt: A0A1B1AYF2
Ligands: SF4, SAM, CL
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Cytosylglucuronate decarboxylase	protein	327	39% helix, 16% strand	A0A1B1AYF2

Ligands and binding sites

SF4 · Iron/sulfur cluster · ligand · 2 copies · chains C
SAM · S-adenosylmethionine · ligand · chains C
CL · Chloride ion · ion · chains C
GOL · Glycerol · additive · 6 copies · chains C

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	681	0.81	0.85	58	SF4, SAM, GOL

Compared structures

7VOB · The crystal structure of a Radical SAM Enzyme BlsE involved in the Biosynthesis of… · the same entry in another collection · chain C against C, 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 A0A1B1AYF2
Elsewhere: RCSB PDB 7VOB · PDBe 7VOB · UniProt A0A1B1AYF2

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