Structure of PDB 1hbz Chain A

Receptor sequence
>1hbzA (length=498) Species: 1270 (Micrococcus luteus) [Search protein sequence]
TTPHATGSTRQNGAPAVSDRQSLTVGSEGPIVLHDTHLLETHQHFNRMNI
PERRPHAKGSGAFGEFEVTEDVSKYTKALVFQPGTKTETLLRFSTVAGEL
GSPDTWRDVRGFALRFYTEEGNYDLVGNNTPIFFLRDPMKFTHFIRSQKR
LPDSGLRDATMQWDFWTNNPESAHQVTYLMGPRGLPRTWREMNGYGSHTY
LWVNAQGEKHWVKYHFISQQGVHNLSNDEATKIAGENADFHRQDLFESIA
KGDHPKWDLYIQAIPYEEGKTYRFNPFDLTKTISQKDYPRIKVGTLTLNR
NPKNHFAQIESAAFSPSNTVPGIGLSPDRMLLGRAFAYHDAQLYRVGAHV
NQLPVNRPKNAVHNYAFEGQMWYDHTGDRSTYVPNSNGDSWSDETGPVDD
GWEADGTLTREAQALRADDDDFGQAGTLVREVFSDQERDDFVETVAGALK
GVRQDVQARAFEYWKNVDATIGQRIEDEVKRHEGDGIPGVEAGGEARI
3D structure
PDB1hbz Three-Dimensional Structure of Catalase from Micrococcus Lysodeikticus at 1.5A Resolution
ChainA
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) H61 N133 S320
Catalytic site (residue number reindexed from 1) H56 N128 S315
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 R58 R59 P60 H61 R97 V131 G132 N133 P143 F146 S202 F319 M335 R339 Y343 Q347 R350 R53 R54 P55 H56 R92 V126 G127 N128 P138 F141 S197 F314 M330 R334 Y338 Q342 R345
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: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:1hbz, PDBe:1hbz, PDBj:1hbz
PDBsum1hbz
PubMed1426241
UniProtP29422|CATA_MICLU Catalase (Gene Name=katA)

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