Structure of PDB 3nwl Chain D

Receptor sequence
>3nwlD (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
ChainD
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 D R71 V73 H74 R111 V145 N147 F160 S216 F333 M349 R353 Y357 T360 H361 R364 R69 V71 H72 R109 V143 N145 F158 S214 F331 M347 R351 Y355 T358 H359 R362
BS02 NDP D F197 S200 R202 K236 V301 P303 H304 Q441 F445 V449 F195 S198 R200 K234 V299 P301 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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