MolNFT v1 · #157530 · protein

Structure of D-ORNITHINE/D-lysine decarboxylase from salmonella typhimurium

6N2H: “Structure of D-ORNITHINE/D-lysine decarboxylase from salmonella typhimurium”. X-ray diffraction, 3 pockets (best druggability 0.43). MolNFT v1 #157530 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6N2H
Type: protein
Length: 459 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-ORNITHINE/D-lysine decarboxylase
UniProt: A0A0D6FAR3
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-ORNITHINE/D-lysine decarboxylase	protein	459	35% helix, 24% strand	A0A0D6FAR3

Ligands and binding sites

DIO · 1,4-diethylene dioxide · additive · 6 copies · chains A
DMS · Dimethyl sulfoxide · additive · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.43	0.75	25	DIO
2	81	0.40	0.78	13	DIO
3	86	0.34	0.74	18	empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

6N2H · Structure of D-ornithine/D-lysine decarboxylase from Salmonella typhimurium · 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 A0A0D6FAR3
Elsewhere: RCSB PDB 6N2H · PDBe 6N2H · UniProt A0A0D6FAR3

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