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Crystal structure of DBR2 with mutation M27L

Analyse Crystal structure of DBR2 with mutation M27L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DY2
Type: protein
Length: 378 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Artemisinic aldehyde DELTA(11(13)) reductase
EC: 1.3.1.92
UniProt: C5H429
Ligands: FMN, DIN
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Artemisinic aldehyde DELTA(11(13)) reductase (EC 1.3.1.92)	protein	378	37% helix, 16% strand	C5H429

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
DIN · 1,6-dihydroxy naphthalene · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	622	0.69	0.77	50	FMN, DIN
2	129	0.58	0.84	29	empty
3	74	0.32	0.74	14	empty

Compared structures

5DY2 · Crystal structure of Dbr2 with mutation M27L · the same entry in another collection · chain A against A, TM-score 1.00
C5H429 · AlphaFold monomer V2.0 prediction for artemisinic aldehyde DELTA(11(13)) reductase… · a predicted model of the same protein · 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 C5H429
Elsewhere: RCSB PDB 5DY2 · PDBe 5DY2 · UniProt C5H429

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