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2.15A resolution structure of sah bound catechol O-methyltransferase (comt) from nannospalax galili

Analyse 2.15A resolution structure of sah bound catechol O-methyltransferase (comt)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AW7
Type: protein
Length: 425 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catechol O-methyltransferase
Ligands: SAH, CA
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catechol O-methyltransferase	protein	213	46% helix, 26% strand	—
B	Catechol O-methyltransferase	protein	212	48% helix, 26% strand	—

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

2 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	509	0.72	0.81	70	CA, SAH
2	471	0.68	0.79	51	CA, SAH

Interfaces

1 interface between chains.

A–B · 2590 Å² buried · 82 hydrogen bonds · protein-protein

Compared structures

6AW7 · 2.15A resolution structure of SAH bound catechol O-methyltransferase (COMT) from… · 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 6AW7 · PDBe 6AW7

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