Structure of PDB 1dgb Chain A

Receptor sequence
>1dgbA (length=498) Species: 9606 (Homo sapiens) [Search protein sequence]
SRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQ
DVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHI
GKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIF
FIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDR
GIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARL
SQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVW
PHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQG
RLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPN
YYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNE
EQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYN
3D structure
PDB1dgb Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H75 N148 D335
Catalytic site (residue number reindexed from 1) H72 N145 D332
Enzyme Commision number 1.11.1.6: catalase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004046 aminoacylase activity
GO:0004096 catalase activity
GO:0004601 peroxidase activity
GO:0016209 antioxidant activity
GO:0016684 oxidoreductase activity, acting on peroxide as acceptor
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0050661 NADP binding
Biological Process
GO:0000302 response to reactive oxygen species
GO:0001649 osteoblast differentiation
GO:0001657 ureteric bud development
GO:0001666 response to hypoxia
GO:0001822 kidney development
GO:0006641 triglyceride metabolic process
GO:0006979 response to oxidative stress
GO:0008203 cholesterol metabolic process
GO:0009060 aerobic respiration
GO:0009410 response to xenobiotic stimulus
GO:0009411 response to UV
GO:0009636 response to toxic substance
GO:0009642 response to light intensity
GO:0009650 UV protection
GO:0010193 response to ozone
GO:0010288 response to lead ion
GO:0014823 response to activity
GO:0014854 response to inactivity
GO:0020027 hemoglobin metabolic process
GO:0032355 response to estradiol
GO:0032868 response to insulin
GO:0033189 response to vitamin A
GO:0033197 response to vitamin E
GO:0033591 response to L-ascorbic acid
GO:0042542 response to hydrogen peroxide
GO:0042744 hydrogen peroxide catabolic process
GO:0043066 negative regulation of apoptotic process
GO:0045471 response to ethanol
GO:0046686 response to cadmium ion
GO:0051781 positive regulation of cell division
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0055093 response to hyperoxia
GO:0061692 cellular detoxification of hydrogen peroxide
GO:0070542 response to fatty acid
GO:0071363 cellular response to growth factor stimulus
GO:0072722 response to amitrole
GO:0080184 response to phenylpropanoid
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005778 peroxisomal membrane
GO:0005782 peroxisomal matrix
GO:0005829 cytosol
GO:0005925 focal adhesion
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0034774 secretory granule lumen
GO:0043231 intracellular membrane-bounded organelle
GO:0062151 catalase complex
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1dgb, PDBe:1dgb, PDBj:1dgb
PDBsum1dgb
PubMed10656833
UniProtP04040|CATA_HUMAN Catalase (Gene Name=CAT)

[Back to BioLiP]