Structure of PDB 2e39 Chain A

Receptor sequence
>2e39A (length=336) Species: 5451 (Agaricales sp. 'Arthromyces ramosus') [Search protein sequence]
SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP
3D structure
PDB2e39 Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosusperoxidase at 100 K refined to 1.3 A resolution: coordination geometries of the ligands to the haem iron
ChainA
Resolution1.3 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) R52 H56 H184 L201
Catalytic site (residue number reindexed from 1) R44 H48 H176 L193
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 MAN A S339 L340 S331 L332
BS02 CA A D57 G75 D77 S79 D49 G67 D69 S71
BS03 CA A S185 D202 T204 V207 D209 S177 D194 T196 V199 D201
BS04 HEM A R48 L51 R52 F55 G155 P156 L180 L181 A183 H184 A187 S188 Q189 E190 G191 M243 R40 L43 R44 F47 G147 P148 L172 L173 A175 H176 A179 S180 Q181 E182 G183 M235
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0140825 lactoperoxidase activity
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:0005576 extracellular region

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2e39, PDBe:2e39, PDBj:2e39
PDBsum2e39
PubMed17372351
UniProtP28313|PER_ARTRA Peroxidase

[Back to BioLiP]