Structure of PDB 1ryi Chain C

Receptor sequence

>1ryiC (length=364) Species: 1423 (Bacillus subtilis)

MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGML
GAHAECEERDAFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAF
SEEDVLQLRQMDDLDSVSWYSKEEVLEKEPYASGDIFGASFIQDDVHVEP
YFVCKAYVKAAKMLGAEIFEHTPVLHVERDGEALFIKTPSGDVWANHVVV
ASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTLYHDHCYIVPR
KSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAG
LRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKE
VNQDWLHAFRIDRK

3D structure

• PDB: 1ryi Structure-function correlation in glycine oxidase from Bacillus subtilis
• Chain: C
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A47 G48 M49
• Catalytic site (residue number reindexed from 1): A47 G48 M49
• Enzyme Commision number: 1.4.3.19: glycine oxidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	C	G13 I15 E34 S35 R41 T42 T43 A46 A47 G48 M49 V174 S202 G203 W205 G300 H327 R329 N330 G331 I332	G13 I15 E34 S35 R41 T42 T43 A46 A47 G48 M49 V174 S202 G203 W205 G300 H327 R329 N330 G331 I332
BS02	GOA	C	Y246 R302 R329	Y246 R302 R329

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0043799 glycine oxidase activity
• GO:0050660 flavin adenine dinucleotide binding
• GO:0071949 FAD binding

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0009228 thiamine biosynthetic process
• GO:0009229 thiamine diphosphate biosynthetic process
• GO:0009635 response to herbicide

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1ryi, PDBe:1ryi, PDBj:1ryi
• PDBsum: 1ryi
• PubMed: 15105420
• UniProt: O31616|GLYOX_BACSU Glycine oxidase (Gene Name=thiO)