MolNFT v1 · #166615 · protein

Crystal structure of apo atmm

6UVQ · D-glucose O-methyltransferase: “Crystal structure of apo atmm”. X-ray diffraction, 1 ligand (MG), 4 pockets (best druggability 0.73). MolNFT v1 #166615 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6UVQ
Type: protein
Length: 514 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-glucose O-methyltransferase
UniProt: Q0H2W9
Ligands: MG
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	D-glucose O-methyltransferase	protein	257	46% helix, 22% strand	Q0H2W9

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	328	0.73	0.85	42	MG
2	464	0.72	0.82	59	MG
3	241	0.70	0.86	53	ACT
4	120	0.69	0.91	33	ACT

Interfaces

1 interface between chains.

A–B · 1178 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6UVQ · Crystal structure of Apo AtmM · 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 Q0H2W9
Elsewhere: RCSB PDB 6UVQ · PDBe 6UVQ · UniProt Q0H2W9

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