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9BDJ

MicroED structure of bovine liver catalase with missing cone eliminated by suspended drop

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0051781biological_processpositive regulation of cell division
A0061692biological_processcellular detoxification of hydrogen peroxide
A0062151cellular_componentcatalase complex
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0051781biological_processpositive regulation of cell division
B0061692biological_processcellular detoxification of hydrogen peroxide
B0062151cellular_componentcatalase complex
C0004096molecular_functioncatalase activity
C0004601molecular_functionperoxidase activity
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005777cellular_componentperoxisome
C0005782cellular_componentperoxisomal matrix
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0019899molecular_functionenzyme binding
C0020037molecular_functionheme binding
C0042542biological_processresponse to hydrogen peroxide
C0042744biological_processhydrogen peroxide catabolic process
C0046872molecular_functionmetal ion binding
C0051781biological_processpositive regulation of cell division
C0061692biological_processcellular detoxification of hydrogen peroxide
C0062151cellular_componentcatalase complex
D0004096molecular_functioncatalase activity
D0004601molecular_functionperoxidase activity
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005777cellular_componentperoxisome
D0005782cellular_componentperoxisomal matrix
D0006979biological_processresponse to oxidative stress
D0016491molecular_functionoxidoreductase activity
D0019899molecular_functionenzyme binding
D0020037molecular_functionheme binding
D0042542biological_processresponse to hydrogen peroxide
D0042744biological_processhydrogen peroxide catabolic process
D0046872molecular_functionmetal ion binding
D0051781biological_processpositive regulation of cell division
D0061692biological_processcellular detoxification of hydrogen peroxide
D0062151cellular_componentcatalase complex
Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFAYpDTH
ChainResidueDetails
AARG353-HIS361

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG
ChainResidueDetails
APHE63-GLY79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7328661
ChainResidueDetails
AHIS74
BHIS74
CHIS74
DHIS74

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
ChainResidueDetails
AASN147
BASN147
CASN147
DASN147

site_idSWS_FT_FI3
Number of Residues44
DetailsBINDING: BINDING => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC
ChainResidueDetails
AHIS193
ATHR444
APHE445
BHIS193
BPHE197
BSER200
BARG202
BTYR214
BLYS236
BTRP302
BHIS304
APHE197
BGLN441
BTHR444
BPHE445
CHIS193
CPHE197
CSER200
CARG202
CTYR214
CLYS236
CTRP302
ASER200
CHIS304
CGLN441
CTHR444
CPHE445
DHIS193
DPHE197
DSER200
DARG202
DTYR214
DLYS236
AARG202
DTRP302
DHIS304
DGLN441
DTHR444
DPHE445
ATYR214
ALYS236
ATRP302
AHIS304
AGLN441

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04040
ChainResidueDetails
AASN212
BASN212
CASN212
DASN212

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10417406, ECO:0007744|PDB:4BLC
ChainResidueDetails
ATYR357
BTYR357
CTYR357
DTYR357

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N-acetylalanine; alternate => ECO:0000250|UniProtKB:P04040
ChainResidueDetails
AALA1
BALA1
CALA1
DALA1

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04040
ChainResidueDetails
ASER8
ASER516
BSER8
BSER516
CSER8
CSER516
DSER8
DSER516

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS12
ALYS220
BLYS12
BLYS220
CLYS12
CLYS220
DLYS12
DLYS220

site_idSWS_FT_FI9
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS232
ALYS498
BLYS232
BLYS498
CLYS232
CLYS498
DLYS232
DLYS498

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ASER416
ASER433
BSER416
BSER433
CSER416
CSER433
DSER416
DSER433

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270
ChainResidueDetails
ALYS448
ALYS479
BLYS448
BLYS479
CLYS448
CLYS479
DLYS448
DLYS479

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04040
ChainResidueDetails
ATHR510
BTHR510
CTHR510
DTHR510

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PDB entries from 2025-06-11

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