Structure of PDB 1ryi Chain D

Receptor sequence
>1ryiD (length=364) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGML
GAHAECEERDAFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAF
SEEDVLQLRQMDDLDSVSWYSKEEVLEKEPYASGDIFGASFIQDDVHVEP
YFVCKAYVKAAKMLGAEIFEHTPVLHVERDGEALFIKTPSGDVWANHVVV
ASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTLYHDHCYIVPR
KSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAG
LRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKE
VNQDWLHAFRIDRK
3D structure
PDB1ryi Structure-function correlation in glycine oxidase from Bacillus subtilis
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D I10 G11 G13 I15 E34 S35 R41 T42 T43 A46 A47 G48 M49 V174 S202 W205 F209 G300 R302 H327 R329 N330 G331 I332 I10 G11 G13 I15 E34 S35 R41 T42 T43 A46 A47 G48 M49 V174 S202 W205 F209 G300 R302 H327 R329 N330 G331 I332
BS02 GOA D 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

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Cellular Component
External links
PDB RCSB:1ryi, PDBe:1ryi, PDBj:1ryi
PDBsum1ryi
PubMed15105420
UniProtO31616|GLYOX_BACSU Glycine oxidase (Gene Name=thiO)

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