MolNFT v1 · #104029 · protein

Human apo-comt, single domain swap

4PYJ · Catechol O-methyltransferase: “Human apo-comt, single domain swap”. X-ray diffraction, 3 ligands (NA, MG, CL), 3 pockets (best druggability 0.69). MolNFT v1 #104029 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4PYJ
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catechol O-methyltransferase
EC: 2.1.1.6
UniProt: P21964
Ligands: NA, MG, CL
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catechol O-methyltransferase (EC 2.1.1.6)	protein	208	50% helix, 15% strand	P21964

Ligands and binding sites

NA · Sodium ion · metal · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · chains A

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

Pockets

3 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	312	0.69	0.83	37	empty
2	93	0.49	0.82	24	CL
3	62	0.35	0.77	18	empty

Compared structures

4PYJ · human apo-COMT, single domain swap · the same entry in another collection · chain A against A, TM-score 1.00
P21964 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P21964) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 P21964
Elsewhere: RCSB PDB 4PYJ · PDBe 4PYJ · UniProt P21964

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