MolNFT v1 · #175600 · protein

Crystal structure of catechol O-methyl transferase (comt) from niastella koreensis

7CVV · O-methyltransferase family 3: “Crystal structure of catechol O-methyl transferase (comt) from niastella koreensis”. X-ray diffraction, 1 ligand (SAM), 8 pockets (best druggability 0.76). MolNFT v1 #175600 on GenesisL1: 3D structure…

PDB: 7CVV
Type: protein
Length: 657 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: O-methyltransferase family 3
UniProt: G8T6H8
Ligands: SAM
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	O-methyltransferase family 3	protein	219	44% helix, 19% strand	G8T6H8

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · 3 copies · chains A, B, C

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.76	0.96	34	empty
2	260	0.58	0.78	53	SAM
3	183	0.51	0.78	35	SAM
4	155	0.48	0.77	29	SAM
5	171	0.47	0.76	22	empty

Interfaces

2 interfaces between chains.

A–C · 1920 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 678 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

7CVV · Crystal structure of Catechol o-methyl transferase (COMT) from Niastella koreensis · 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 G8T6H8
Elsewhere: RCSB PDB 7CVV · PDBe 7CVV · UniProt G8T6H8

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