Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8PVD

Structure of catalase determined by cryoEM at 100 keV

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0001649biological_processosteoblast differentiation
A0001657biological_processureteric bud development
A0001666biological_processresponse to hypoxia
A0001822biological_processkidney development
A0004046molecular_functionaminoacylase activity
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005778cellular_componentperoxisomal membrane
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006641biological_processtriglyceride metabolic process
A0006979biological_processresponse to oxidative stress
A0008203biological_processcholesterol metabolic process
A0009060biological_processaerobic respiration
A0009410biological_processresponse to xenobiotic stimulus
A0009411biological_processresponse to UV
A0009636biological_processresponse to toxic substance
A0009642biological_processresponse to light intensity
A0009650biological_processUV protection
A0010193biological_processresponse to ozone
A0010288biological_processresponse to lead ion
A0014823biological_processresponse to activity
A0014854biological_processresponse to inactivity
A0016020cellular_componentmembrane
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0016684molecular_functionoxidoreductase activity, acting on peroxide as acceptor
A0019899molecular_functionenzyme binding
A0020027biological_processhemoglobin metabolic process
A0020037molecular_functionheme binding
A0032355biological_processresponse to estradiol
A0032868biological_processresponse to insulin
A0032991cellular_componentprotein-containing complex
A0033189biological_processresponse to vitamin A
A0033197biological_processresponse to vitamin E
A0033591biological_processresponse to L-ascorbic acid
A0034774cellular_componentsecretory granule lumen
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043066biological_processnegative regulation of apoptotic process
A0045471biological_processresponse to ethanol
A0046686biological_processresponse to cadmium ion
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
A0051781biological_processpositive regulation of cell division
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0055093biological_processresponse to hyperoxia
A0061692biological_processcellular detoxification of hydrogen peroxide
A0062151cellular_componentcatalase complex
A0070062cellular_componentextracellular exosome
A0070542biological_processresponse to fatty acid
A0071363biological_processcellular response to growth factor stimulus
A0072722biological_processresponse to amitrole
A0080184biological_processresponse to phenylpropanoid
A1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH
ChainResidueDetails
AARG354-HIS362

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG
ChainResidueDetails
APHE64-GLY80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10656833
ChainResidueDetails
AHIS75
AASN148

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
ChainResidueDetails
AHIS194
ASER201
AARG203
AASN213
ATRP303
AHIS305

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGH
ChainResidueDetails
ALYS237

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF
ChainResidueDetails
ALYS306

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10656833, ECO:0000269|PubMed:10666617, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH, ECO:0007744|PDB:1F4J, ECO:0007744|PDB:1QQW
ChainResidueDetails
ATYR358

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER9
ASER422
ASER517

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS221

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS233
ALYS499

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS306
ALYS480

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ASER417

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR511

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER515

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon