Structure of PDB 1mn2 Chain A

Receptor sequence
>1mn2A (length=357) [Search protein sequence]
AVCPDGTRVSHAACCAFIPLAQDLQETIFQNECGQDAHEVIRLTFHDAIA
ISRSQGPKAGGGADGSMLLFPTVEPNFSANNGIDDSVNNLIPFMQKHNTI
SAADLVQFAGAVALSNCPGAPRLEFLAGRPNKTIAAVDGLIPEPQDSVTK
ILQRFEDAGGFTPFEVVSLLASHSVARANKVDQTIDAAPFDSTPFTFDTQ
VFLEVLLKGVGFPGSANNTGEVASPLPLGSGSDTGEMRLQSDFALAHDPR
TACIWQGFVNEQAFMAASFRAAMSKLAVLGHNRNSLIDCSDVVPVPKPAT
GQPAMFPASTGPQDLELSCPSERFPTLTTQPGASQSLIAHCPDGSMSCPG
VQFNGPA
3D structure
PDB1mn2 Crystal structures of substrate binding site mutants of manganese peroxidase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R42 H46 H173 F190 D242
Catalytic site (residue number reindexed from 1) R42 H46 H173 F190 D242
Enzyme Commision number 1.11.1.13: manganese 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 S174 D191 T193 T196 D198 S174 D191 T193 T196 D198
BS02 CA A D47 G62 D64 S66 D47 G62 D64 S66
BS03 HEM A H38 I41 R42 F45 E143 P144 L170 S172 H173 A176 R177 A178 N179 K180 V181 F190 L239 H38 I41 R42 F45 E143 P144 L170 S172 H173 A176 R177 A178 N179 K180 V181 F190 L239
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016689 manganese 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:0046274 lignin catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:1mn2, PDBe:1mn2, PDBj:1mn2
PDBsum1mn2
PubMed9211904
UniProtQ02567|PEM1_PHACH Manganese peroxidase 1 (Gene Name=MNP1)

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