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Agao holoenzyme at 1.55 ångströms

Analyse Agao holoenzyme at 1.55 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1W6G
Type: protein
Length: 620 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phenylethylamine oxidase
EC: 1.4.3.6
UniProt: P46881
Ligands: CU, NA, SO4
Pockets: 6 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylethylamine oxidase (EC 1.4.3.6)	protein	620	13% helix, 42% strand	P46881

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 5 copies · chains A

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

Pockets

6 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	55	0.66	0.95	26	empty
2	277	0.64	0.81	47	empty
3	183	0.50	0.76	25	empty
4	68	0.43	0.81	16	empty
5	78	0.34	0.75	20	empty

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

1W6G · AGAO holoenzyme at 1.55 angstroms · 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 1W6G · PDBe 1W6G · UniProt P46881

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