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1.50A resolution structure of catechol O-methyltransferase (comt) from nannospalax galili

Analyse 1.50A resolution structure of catechol O-methyltransferase (comt) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AW4
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catechol O-methyltransferase
Ligands: NA, PO4
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catechol O-methyltransferase	protein	213	46% helix, 23% strand	—

Ligands and binding sites

NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	221	0.62	0.81	28	TRS, PO4
2	60	0.40	0.81	15	PO4

Compared structures

6AW4 · 1.50A resolution structure of catechol O-methyltransferase (COMT) from Nannospalax galili · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 6AW4 · PDBe 6AW4

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