Structure of PDB 6rjr Chain D

Receptor sequence
>6rjrD (length=502) Species: 28985 (Kluyveromyces lactis) [Search protein sequence]
GHPTNTADVRKDRVVTNSQGAPINEPFATQRVGQHGPLLLQDFNLLDSLA
HFNRERIPERNPHAHGSGAFGYLEITDDITDVCGSAMFDTVGKRTRCLVR
FSTVGGEKGSADTARDPRGFAIKFYSEEGNVDWVNNNTPVFFIRDPSKFP
HFIHTQKRNPETNMKDADMFWDFLTTEENQVAIHQVMILFSDRGTPASYR
NMNSYSGHTYKWSNKQGEWRYVQVHLKTDQGIKNLNNEEATKLAGENPDY
CQKDLFENIAKGNYPSWTLYIQTMTEEEAEKLPFSVFDLTKVWPHKQFPL
RRVGKMVLNENPENYFAQVEQAAFSPSHTVPYQEASADPVLQARLFSYPD
AHRYRLGPNYSQIPVNCPYASKVFNPAIRDGPMNVNGNLGKEPNYLSTSK
KYQFIQQSKPIQQHQEVWSGPAMPVHWATSPGDIDFVQARDLYNKVLSKQ
PGQQKALAHNVAVHVASACPEIQDRVFAMFARVDRGLSENIKKEALSLSP
RK
3D structure
PDB6rjr Peroxisomal catalases from the yeasts Pichia pastoris and Kluyveromyces lactis as models for oxidative damage in higher eukaryotes.
ChainD
Resolution1.895 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.6: catalase.
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 D R61 N62 H64 R101 V135 N137 F150 F325 V341 R345 Y349 A352 H353 R356 R60 N61 H63 R100 V134 N136 F149 F324 V340 R344 Y348 A351 H352 R355
BS02 NDP D P140 H185 S192 R194 K228 V293 H296 Q439 V447 Q451 P139 H184 S191 R193 K227 V292 H295 Q438 V446 Q450
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6rjr, PDBe:6rjr, PDBj:6rjr
PDBsum6rjr
PubMed31238127
UniProtQ6CR58

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