Structure of PDB 1sy7 Chain B

Receptor sequence
>1sy7B (length=698) Species: 5141 (Neurospora crassa) [Search protein sequence]
ARLTTDYGVKQTTADDWLRIVSDDKIGPSLLEDPFARERIMRFDHERIPE
RVVHARGSGAFGKFKVYESASDLTMAPVLTDTSRETPVFVRFSTVLGSRG
SADTVRDVRGFAVKFYTEEGNWDLVGNNIPVFFIQDAIKFPDVIHAGKPE
PHNEVPQAQSAHNNFWDFQFNHTEATHMFTWAMSDRAIPRSLRMMQGFGV
NTYTLINAQGKRHFVKFHWTPELGVHSLVWDEALKLAGQDPDFHRKDLWE
AIENGAYPKWKFGIQAIAEEDEHKFDFDILDATKIWPEDLVPVRYIGEME
LNRNPDEFFPQTEQIAFCTSHVVNGIGFSDDPLLQGRNFSYFDTQISRLG
VNFQELPINRPVCPVMNFNRDGAMRHTISRGTVNYYPNRFDACPPASLKE
GGYLEYAQKVAGIKARARSAKFKEHFSQAQLFYNSMSPIEKQHMINAFGF
ELDHCEDPVVYGRMVQRLADIDLGLAQTIAEMVGGEAPTTTNHPNHGRKT
INLSQTEFPPATPTIKSRRVAIIIADGYDNVAYDAAYAAISANQAIPLVI
GPRRSKVTAANGSTVQPHHHLEGFRSTMVDAIFIPGGAKAAETLSKNGRA
LHWIREAFGHLKAIGATGEAVDLVAKAIALPQVTVSSEAEVHESYGVVTL
KKVKPESFTDAVKIAKGAAGFLGEFFYAIAQHRNWDRELDGLHSMIAY
3D structure
PDB1sy7 Unusual Cys-Tyr covalent bond in a large catalase
ChainB
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H92 N165 C356
Catalytic site (residue number reindexed from 1) H54 N127 C318
Enzyme Commision number 1.11.1.6: catalase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004096 catalase 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:0048315 conidium formation
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005619 ascospore wall
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:1sy7, PDBe:1sy7, PDBj:1sy7
PDBsum1sy7
PubMed15342250
UniProtQ9C168|CAT1_NEUCR Catalase-1 (Gene Name=cat-1)

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