Structure of PDB 4aul Chain D

Receptor sequence
>4aulD (length=671) Species: 85995 (Mycothermus thermophilus) [Search protein sequence]
SPLAAYEVDDSTGYLTSDVGGPIQDQTSLKAGIRGPTLLEDFMFRQKIQH
FDHERVPERAVNARGAGAHGTFTSYADWSNITAASFLNATGKQTPVFVRF
STVAGSRGSADTARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAIQFPD
LIHSVKPRPDNEIPQAATAHDSAWDFFSQQPSTMHTLFWAMSGHGIPRSY
RHMDGFGVHTFRFVKDDGSSKLIKWHFKSRQGKASLVWEEAQVLSGKNAD
FHRQDLWDAIESGNGPEWDVCVQIVDESQAQAFGFDLLDPTKIIPEEYAP
LTKLGLLKLDRNPTNYFAETEQVMFQPGHIVRGIDFTEDPLLQGRLFSYL
DTQLNRNGGPNFEQLPINMPRVPIHNNNRDGAGQMFIHRNKYPYTPNTLN
SGYPRQANQNAGRGFFTAPGRTASGALVREVSPTFNDHWSQPRLFFNSLT
PVEQQFLVNAMRFEISLVKSEEVKKNVLTQLNRVSHDVAVRVAAAIGLGA
PDADDTYYHNNKTAGVSIVGSGPLPTIKTLRVGILATTSESSALDQAAQL
RTRLEKDGLVVTVVAETLREGVDQTYSTADATGFDGVVVVDGAAALFSSP
LFPTGRPLQIFVDAYRWGKPVGVCGSEVLDAADVPEDGDGVYSEESVDMF
VEEFEKGLATFRFTDRFALDS
3D structure
PDB4aul Structure, Recombinant Expression and Mutagenesis Studies of the Catalase with Oxidase Activity from Scytalidium Thermophilum
ChainD
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N82 N155 Q346
Catalytic site (residue number reindexed from 1) N62 N135 Q326
Enzyme Commision number 1.11.1.6: catalase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004097 catechol oxidase activity
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006979 response to oxidative stress
GO:0042744 hydrogen peroxide catabolic 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:4aul, PDBe:4aul, PDBj:4aul
PDBsum4aul
PubMed23519415
UniProtM4GGR6

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