Structure of PDB 8wzh Chain A

Receptor sequence
>8wzhA (length=497) Species: 9606 (Homo sapiens) [Search protein sequence]
RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQD
VVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIG
KKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFF
IRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG
IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLS
QEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWP
HKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGR
LFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY
YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEE
QRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYN
3D structure
PDB8wzh Factors affecting macromolecule orientations in thin films formed in cryo-EM.
ChainA
Resolution3.7 Å
3D
structure
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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 V74 H75 R112 V146 N148 P158 F161 F334 R354 Y358 T361 H362 R365 V70 H71 R108 V142 N144 P154 F157 F330 R350 Y354 T357 H358 R361
BS02 NDP A P151 F198 R203 V302 W303 P304 H305 F446 V450 P147 F194 R199 V298 W299 P300 H301 F442 V446
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8wzh, PDBe:8wzh, PDBj:8wzh
PDBsum8wzh
PubMed38935342
UniProtP04040|CATA_HUMAN Catalase (Gene Name=CAT)

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