Structure of PDB 3q3u Chain A

Receptor sequence

>3q3uA (length=338) [Search protein sequence]

MVSCGGGRSVKNAACCAWFPVLDDIQANLFNGGKCEEEAHEAVRLTFHDA
VGFSLAAQKAGKFGGGGADGSILAFSDIETAFIPNFGLEFTTEGFIPFAL
AHGVSFGDFVQFAGAVGAANCAGGPRLQFLAGRSNISQPSPDGLVPDPTD
SADKILARMADIGFSPTEVVHLLASHSIAAQYEVDTDVAGSPFDSTPSVF
DTQFFVESLLHGTQFTGSGQGGEVMSPIPGEFRLQSDFALSRDPRTACEW
QALVNNQQAMVNNFEAVMSRLAVIGQIPSELVDCSDVIPTPPLAKVAQVG
SLPPGKSMADVQVACTNGMPFPSLPTSPGPVQTVAPVL

3D structure

PDB

3q3u Crystallographic, kinetic, and spectroscopic study of the first ligninolytic peroxidase presenting a catalytic tyrosine.

Chain

Resolution

1.85 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

1.11.1.-

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)
BS01	HEM	A	H39 E40 V42 R43 F46 D146 P147 L171 S174 H175 A178 A179 Q180 Y181 E182 V183 F192 L233 S235	H40 E41 V43 R44 F47 D147 P148 L172 S175 H176 A179 A180 Q181 Y182 E183 V184 F193 L234 S236
BS02	CA	A	D48 G66 D68 S70	D49 G67 D69 S71
BS03	CA	A	S176 D193 T195 V198 D200	S177 D194 T196 V199 D201

Gene Ontology

	Molecular Function
GO:0004601	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

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3q3u, PDBe:3q3u, PDBj:3q3u
PDBsum	3q3u
PubMed	21367853
UniProt	Q60FD2

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