Structure of PDB 3nwl Chain C

Receptor sequence
>3nwlC (length=499) Species: 9913 (Bos taurus) [Search protein sequence]
NRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQ
DVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHI
GKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIF
FIRDALLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDR
GIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIKNLSVEDAARL
AHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVW
PHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQG
RLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPN
YYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQVRTFYLKVLNE
EQRKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPEYGSRIQALLDKYNE
3D structure
PDB3nwl Polymer-Induced Heteronucleation for Protein Single Crystal Growth: Structural Elucidation of Bovine Liver Catalase and Concanavalin A Forms
ChainC
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H74 N147 D334
Catalytic site (residue number reindexed from 1) H72 N145 D332
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 C R71 H74 R111 V145 N147 F160 S216 F333 M349 R353 Y357 T360 H361 R364 R69 H72 R109 V143 N145 F158 S214 F331 M347 R351 Y355 T358 H359 R362
BS02 NDP C H193 F197 R202 K236 V301 H304 Q441 F445 V449 H191 F195 R200 K234 V299 H302 Q439 F443 V447
Gene Ontology
Molecular Function
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0019899 enzyme 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:0051781 positive regulation of cell division
GO:0061692 cellular detoxification of hydrogen peroxide
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005782 peroxisomal matrix
GO:0062151 catalase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3nwl, PDBe:3nwl, PDBj:3nwl
PDBsum3nwl
PubMed
UniProtP00432|CATA_BOVIN Catalase (Gene Name=CAT)

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