Structure of PDB 3mm2 Chain A

Receptor sequence
>3mm2A (length=439) Species: 5331 (Bjerkandera adusta) [Search protein sequence]
TILPLNNIQGDILVGMKKQKERFVFFQVNDATSFKTALKTYVPERITSAA
ILISDPSQQPLAFVNLGFSNTGLQALGITDDLGDAQFPDGQFADAANLGD
DLSQWVAPFTGTTIHGVFLIGSDQDDFLDQFTDDISSTFGSSITQVQALS
GSARPGDQAGHEHFGFLDGISQPSVTGWETTVFPGQAVVPPGIILTGRDG
DTGTRPSWALDGSFMAFRHFQQKVPEFNAYTLANAIPANSAGNLTQQEGA
EFLGARMFGRWKSGAPIDLAPTADDPALGADPQRNNNFDYSDTLTDETRC
PFGAHVRKTNPRQDLGGPVDTFHAMRSSIPYGPETSDAELASGVTAQDRG
LLFVEYQSIIGNGFRFQQINWANNANFPFSKPITPGIEPIIGQTTPRTVG
GLDPLNQNETFTVPLFVIPKGGEYFFLPSISALTATIAA
3D structure
PDB3mm2 The catalytic mechanism of dye-decolorizing peroxidase DyP may require the swinging movement of an aspartic acid residue
ChainA
Resolution1.45 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.19: dye decolorizing 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 A E165 L170 I173 S174 F223 Q225 F261 R263 H308 V309 T312 N313 R329 L354 F356 F367 Q370 I394 V420 E162 L167 I170 S171 F220 Q222 F258 R260 H305 V306 T309 N310 R326 L351 F353 F364 Q367 I391 V417
BS02 CYN A R329 F356 R326 F353
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3mm2, PDBe:3mm2, PDBj:3mm2
PDBsum3mm2
PubMed21569205
UniProtQ8WZK8

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