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Crystal structure of the alpha subunit of heme dependent oxidative N- demethylase (hodm)

Analyse Crystal structure of the alpha subunit of heme dependent oxidative N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LTE
Type: protein
Length: 333 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme dependent oxidative N-demethylase
UniProt: A4XXY9
Ligands: HEM, ETX, NA
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme dependent oxidative N-demethylase	protein	333	36% helix, 23% strand	A4XXY9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
ETX · 2-ethoxyethanol · ligand · chains A
NA · Sodium ion · metal

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	397	0.82	0.90	50	HEM
2	57	0.67	0.96	23	empty
3	107	0.36	0.74	26	empty

Compared structures

5LTE · Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM) · 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 A4XXY9
Elsewhere: RCSB PDB 5LTE · PDBe 5LTE · UniProt A4XXY9

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