MolNFT v1 · #159186 · protein

Crystal structure of (E)-biformene synthase lrdc from streptomyces sp. strain K155 in complex with mg

6OH7 · Labdane-related diterpene synthase: “Crystal structure of (E)-biformene synthase lrdc from streptomyces sp. strain K155 in complex with mg”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.77). MolNFT v1 #159186 on…

PDB: 6OH7
Type: protein
Length: 311 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Labdane-related diterpene synthase
EC: 4.2.3.193
UniProt: A0A158RFK9
Ligands: MG
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Labdane-related diterpene synthase (EC 4.2.3.193)	protein	311	71% helix, 0% strand	A0A158RFK9

Ligands and binding sites

MG · Magnesium ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A

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

Pockets

2 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	494	0.77	0.85	59	MG
2	111	0.42	0.76	21	empty

Compared structures

6OH7 · Crystal structure of (E)-biformene synthase LrdC from Streptomyces sp. strain K155 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 A0A158RFK9
Elsewhere: RCSB PDB 6OH7 · PDBe 6OH7 · UniProt A0A158RFK9

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