Structure of PDB 1bgp Chain A

Receptor sequence

>1bgpA (length=309) Species: 4513 (Hordeum vulgare)

AEPPVAPGLSFDFYWQTCPRAESIVREFVQEAVRKDIGLAAGLLRLHFHD
CFVQGCDASVLLDGSATGPGEQQAPPNLTLRPSAFKAVNDIRDRLERECR
GAVVSCSDILALAARDSVVVSGGPDYRVPLGRRDSRSFASTQDVLSDLPG
PSSNVQSLLALLGRLGLDATDLVTISGGHTIGLAHCSSFEDRLFPRPDPT
ISPTFLSRLKRTCPAKGTDRRTVLDVRTPNVFDNKYYIDLVNREGLFVSD
QDLFTNAITRPIVERFAQSQQDFFEQFGVSIGKMGQMRVRTSDQGEVRRN
CSVRNPGPG

3D structure

• PDB: 1bgp Structure of barley grain peroxidase refined at 1.9-A resolution. A plant peroxidase reversibly inactivated at neutral pH.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R45 H49 N77 H179 D250
• Catalytic site (residue number reindexed from 1): R45 H49 N77 H179 D250
• 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	CA	A	T180 D225 T228 V231 D233	T180 D225 T228 V231 D233
BS02	NA	A	D50 V53 Q54 G55 D57 S59	D50 V53 Q54 G55 D57 S59
BS03	HEM	A	A41 L44 R45 F48 R81 P149 G150 P151 I175 G178 H179 G182 L183 A184 H185 S188 L224 F247	A41 L44 R45 F48 R81 P149 G150 P151 I175 G178 H179 G182 L183 A184 H185 S188 L224 F247

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:1bgp, PDBe:1bgp, PDBj:1bgp
• PDBsum: 1bgp
• PubMed: 9442067
• UniProt: Q40069