MolNFT v1 · #50376 · protein

Structure of alpha-glycerophosphate oxidase from streptococcus sp.: a template for the mitochondrial alpha- glycerophosphate dehydrogenase

2RGH: “Structure of alpha-glycerophosphate oxidase from streptococcus sp.: a template for the mitochondrial alpha…”. X-ray diffraction, 2 ligands (FAD, SO4), 7 pockets (best druggability 0.79). MolNFT v1 #50376 on GenesisL1: 3D structure…

PDB: 2RGH
Type: protein
Length: 546 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-glycerophosphate oxidase
EC: 1.1.3.21
Ligands: FAD, SO4
Pockets: 7 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-glycerophosphate oxidase (EC 1.1.3.21)	protein	546	43% helix, 19% strand	—

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

7 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	617	0.79	0.85	77	SO4, FAD
2	169	0.66	0.86	26	empty
3	125	0.62	0.86	22	empty
4	158	0.48	0.77	25	empty
5	119	0.40	0.75	20	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

2RGH · Structure of Alpha-Glycerophosphate Oxidase from Streptococcus sp.: A Template for the… · 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
Elsewhere: RCSB PDB 2RGH · PDBe 2RGH

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