Structure of PDB 1apx Chain D

Receptor sequence
>1apxD (length=249) Species: 3888 (Pisum sativum) [Search protein sequence]
GKSYPTVSPDYQKAIEKAKRKLRGFIAEKKCAPLILRLAWHSAGTFDSKT
KTGGPFGTIKHQAELAHGANNGLDIAVRLLEPIKEQFPIVSYADFYQLAG
VVAVEITGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGL
SDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLTGEKDG
LLQLPSDKALLTDSVFRPLVEKYAADEDVFFADYAEAHLKLSELGFAEA
3D structure
PDB1apx Crystal structure of recombinant pea cytosolic ascorbate peroxidase.
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R38 H42 L66 H163 W179 D208
Catalytic site (residue number reindexed from 1) R37 H41 L65 H162 W178 D207
Enzyme Commision number 1.11.1.11: L-ascorbate 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 D P34 W41 A134 F145 L159 H163 G166 A167 A168 H169 R172 S173 W179 P33 W40 A133 F144 L158 H162 G165 A166 A167 H168 R171 S172 W178
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016688 L-ascorbate peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0000302 response to reactive oxygen species
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0009507 chloroplast

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1apx, PDBe:1apx, PDBj:1apx
PDBsum1apx
PubMed7703247
UniProtP48534|APX1_PEA L-ascorbate peroxidase, cytosolic (Gene Name=APX1)

[Back to BioLiP]