MolNFT v1 · #26359 · protein

Crystal structure of amine oxidase complexed with cobalt ion

1WMP · Phenylethylamine oxidase: “Crystal structure of amine oxidase complexed with cobalt ion”. X-ray diffraction, 1 ligand (CO), 20 pockets (best druggability 0.89). MolNFT v1 #26359 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1WMP
Type: protein
Length: 1,240 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylethylamine oxidase
EC: 1.4.3.6
UniProt: P46881
Ligands: CO
Pockets: 20 · best druggability 0.89

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phenylethylamine oxidase (EC 1.4.3.6)	protein	620	13% helix, 43% strand	P46881

Ligands and binding sites

CO · Cobalt (II) ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1080	0.89	0.91	143	empty
2	208	0.68	0.86	43	empty
3	338	0.68	0.82	59	empty
4	317	0.68	0.82	34	empty
5	352	0.67	0.81	35	empty

Interfaces

1 interface between chains.

A–B · 6673 Å² buried · 104 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1WMP · Crystal structure of amine oxidase complexed with cobalt ion · 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 P46881
Elsewhere: RCSB PDB 1WMP · PDBe 1WMP · UniProt P46881

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