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Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579

Analyse Crystal strcuture of glycine oxidase from bacillus cereus atcc 14579 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CYX
Type: protein
Length: 720 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycine oxidase
EC: 1.5.3.-
UniProt: Q81HQ7
Ligands: FAD
Pockets: 8 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycine oxidase (EC 1.5.3.-)	protein	363	33% helix, 29% strand	Q81HQ7
B	Glycine oxidase (EC 1.5.3.-)	protein	357	31% helix, 29% strand	Q81HQ7

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	388	0.83	0.92	62	FAD
2	440	0.83	0.90	71	FAD
3	818	0.74	0.79	85	empty
4	402	0.66	0.79	44	empty
5	292	0.62	0.80	35	empty

Interfaces

1 interface between chains.

A–B · 842 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

7CYX · Crystal strcuture of Glycine oxidase from Bacillus cereus ATCC 14579 · 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 Q81HQ7
Elsewhere: RCSB PDB 7CYX · PDBe 7CYX · UniProt Q81HQ7

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