Structure of PDB 4a5g Chain B

Receptor sequence

>4a5gB (length=307) Species: 3726 (Raphanus sativus)

GGSLNATFYAGTCPNASAMVRTIVQQAFQSDSRIGASLIRLHFHDCFVLG
CDASILLDNSGSIISEKNAGPNANSARGFNVVDNIKTALENACPGVVSCT
DVLALASQASVSLSGGPSWTVDLGRRDTLTANQAGANSSIPSPTQGLSNI
TSKFSAVGLNTNDLVALSGAHTFGRATCGVFSNRLFNFSGKGNPDPTLNT
TLLSTLQELCPQKGRGSGSTNLDLSTPDAFDNNYFTNLQSNNGLLQSDQE
LFSTTGSATIAIVTSFASNQTLFFQAFAQSMINMGNISPLTGSSGEIRLD
CKKTNGS

3D structure

• PDB: 4a5g Crystallographic Structure of the Raphanus Sativus Anionic Peroxidase
• Chain: B
• Resolution: 2.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R40 H44 N72 H171 D248
• Catalytic site (residue number reindexed from 1): R40 H44 N72 H171 D248
• Enzyme Commision number: 1.11.1.7: peroxidase.

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	HEM	B	R33 A36 S37 R40 F43 S75 S142 P143 I150 F154 A170 H171 G174 R175 A176 V180 L222 L245	R33 A36 S37 R40 F43 S75 S142 P143 I150 F154 A170 H171 G174 R175 A176 V180 L222 L245
BS02	CA	B	D45 V48 G50 D52 S54	D45 V48 G50 D52 S54
BS03	CA	B	T172 D223 T226 A229 D231	T172 D223 T226 A229 D231

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0140825 lactoperoxidase activity

Biological Process

• GO:0006979 response to oxidative stress
• GO:0042744 hydrogen peroxide catabolic process
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:4a5g, PDBe:4a5g, PDBj:4a5g
• PDBsum: 4a5g
• UniProt: K7N5L9