Structure of PDB 1qwl Chain A

Receptor sequence
>1qwlA (length=491) Species: 210 (Helicobacter pylori) [Search protein sequence]
MVNKDVKQTTAFGAPVWDDNNVITAGPRGPVLLQSTWFLEKLAAFDRERI
PERVVHAKGSGAYGTFTVTKDITKYTKAKIFSKVGKKTECFFRFSTVAGE
RGSADAVRDPRGFAMKYYTEEGNWDLVGNNTPVFFIRDAIKFPDFIHTQK
RDPQTNLPNHDMVWDFWSNVPESLYQVTWVMSDRGIPKSFRHMDGFGSHT
FSLINAKGERFWVKFHFHTMQGVKHLTNEEAAEIRKHDPDSNQRDLFDAI
ARGDYPKWKLSIQVMPEEDAKKYRFHPFDVTKIWYTQDYPLMEVGIVELN
KNPENYFAEVEQAAFTPANVVPGIGYSPDRMLQGRLFSYGDTHRYRLGVN
YPQIPVNKPRCPFHSSSRDGYMQNGYYGSLQNYTPSSLPGYKEDKSARDP
KFNLAHIEKEFEVWNWDYRADDSDYYTQPGDYYRSLPADEKERLHDTIGE
SLAHVTHKEIVDKQLEHFKKADPKYAEGVKKALEKHQKMMK
3D structure
PDB1qwl Structure of Helicobacter pylori Catalase, with and without Formic Acid Bound, at 1.6 A Resolution
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H56 N129 T316
Catalytic site (residue number reindexed from 1) H56 N129 T316
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 A R53 V55 H56 R93 V127 G128 N129 A139 F142 S198 F315 M331 R335 S338 Y339 T342 H343 R346 R53 V55 H56 R93 V127 G128 N129 A139 F142 S198 F315 M331 R335 S338 Y339 T342 H343 R346
BS02 OXY A H56 F142 H56 F142
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0005515 protein binding
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1qwl, PDBe:1qwl, PDBj:1qwl
PDBsum1qwl
PubMed15023060
UniProtP77872|CATA_HELPY Catalase (Gene Name=katA)

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