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6RJN

Crystal structure of a Fungal Catalase at 2.3 Angstroms

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0000166molecular_functionnucleotide binding
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0000166molecular_functionnucleotide binding
C0004096molecular_functioncatalase activity
C0004601molecular_functionperoxidase activity
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005777cellular_componentperoxisome
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
C0042542biological_processresponse to hydrogen peroxide
C0042744biological_processhydrogen peroxide catabolic process
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
D0000166molecular_functionnucleotide binding
D0004096molecular_functioncatalase activity
D0004601molecular_functionperoxidase activity
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005777cellular_componentperoxisome
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
D0042542biological_processresponse to hydrogen peroxide
D0042744biological_processhydrogen peroxide catabolic process
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEM A 601
ChainResidue
AARG63
APHE152
AHIS209
ALEU290
APHE325
AVAL341
ASER344
AARG345
ASER348
ATYR349
ATHR352
AVAL64
AHIS353
AARG356
AHOH736
AHOH742
AHOH779
DASP56
AVAL65
AHIS66
AARG103
AGLY122
AVAL137
ATYR138
AASN139

site_idAC2
Number of Residues22
Detailsbinding site for residue NDP A 602
ChainResidue
APRO142
AHIS185
ASER192
AARG194
AASN204
ATYR206
AHIS226
ALYS228
ATRP294
APRO295
AHIS296
AGLN441
AALA444
ALEU445
AVAL448
APHE449
AGLN455
AHOH724
AHOH740
AHOH749
AHOH758
AHOH763

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 603
ChainResidue
ATRP446
ALYS447
AGLU488
AHOH813
AHOH904

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 604
ChainResidue
ACYS368
AASN386

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 605
ChainResidue
AGLU22
AGLN44
BLYS212
BTYR214
BGLU416

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 606
ChainResidue
ALYS212
ATYR214
APRO336
AGLU416
BGLU22
BGLN44

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 A 607
ChainResidue
ATHR375
AMET378
AASN386
AASN388
AHOH741

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 A 608
ChainResidue
AARG147
AHIS427
ATRP428
AGLY429
ALEU432
AHOH719

site_idAC9
Number of Residues2
Detailsbinding site for residue CL A 609
ChainResidue
AARG57
CARG57

site_idAD1
Number of Residues4
Detailsbinding site for residue CL A 610
ChainResidue
AGLY454
AARG457
CARG457
CGOL605

site_idAD2
Number of Residues6
Detailsbinding site for residue K A 611
ChainResidue
APRO142
AGLY208
AGLN224
ALYS292
AHOH801
AHOH880

site_idAD3
Number of Residues6
Detailsbinding site for residue NA A 612
ChainResidue
AASN28
AASN34
APRO36
AHOH788
AHOH917
AHOH943

site_idAD4
Number of Residues5
Detailsbinding site for residue K B 601
ChainResidue
AGLN377
AMET378
BSER51
BPHE55
BHOH832

site_idAD5
Number of Residues25
Detailsbinding site for residue HEM B 602
ChainResidue
BARG63
BVAL64
BVAL65
BHIS66
BARG103
BGLY122
BSER124
BTYR138
BASN139
BPHE152
BHIS209
BLEU290
BPHE325
BVAL341
BSER344
BARG345
BSER348
BTYR349
BTHR352
BHIS353
BARG356
BHOH747
BHOH767
BHOH777
CASP56

site_idAD6
Number of Residues21
Detailsbinding site for residue NDP B 603
ChainResidue
BHIS185
BARG194
BASN204
BTYR206
BHIS226
BLYS228
BVAL293
BTRP294
BPRO295
BHIS296
BGLN441
BLEU445
BVAL448
BPHE449
BGLN455
BGOL607
BHOH707
BHOH782
BHOH802
BHOH839
BHOH865

site_idAD7
Number of Residues4
Detailsbinding site for residue GOL B 604
ChainResidue
BARG118
BASN238
BALA241
BGLY242

site_idAD8
Number of Residues4
Detailsbinding site for residue GOL B 605
ChainResidue
BASP169
BASN171
BHOH719
DGOL606

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL B 606
ChainResidue
BASP193
BASN235
BASN237
BGLU240
BGLN455
BHOH862

site_idAE1
Number of Residues4
Detailsbinding site for residue GOL B 607
ChainResidue
BPRO295
BGLN441
BALA444
BNDP603

site_idAE2
Number of Residues6
Detailsbinding site for residue PEG B 608
ChainResidue
BGLN279
BLYS282
BGLN283
BASP298
CPEG608
CHOH838

site_idAE3
Number of Residues2
Detailsbinding site for residue CL B 609
ChainResidue
BARG57
DARG57

site_idAE4
Number of Residues3
Detailsbinding site for residue CL B 610
ChainResidue
BGLY454
BARG457
DHOH851

site_idAE5
Number of Residues6
Detailsbinding site for residue K B 611
ChainResidue
BPRO142
BGLY208
BGLN224
BLYS292
BHOH750
BHOH819

site_idAE6
Number of Residues6
Detailsbinding site for residue NA B 612
ChainResidue
BASN28
BASN34
BPRO36
BHOH762
BHOH967
BHOH994

site_idAE7
Number of Residues4
Detailsbinding site for residue K B 613
ChainResidue
BSER51
BHOH959
CSER150
CHOH805

site_idAE8
Number of Residues25
Detailsbinding site for residue HEM C 601
ChainResidue
BASP56
CARG63
CVAL64
CVAL65
CHIS66
CARG103
CGLY122
CVAL137
CTYR138
CASN139
CPHE152
CHIS209
CPHE325
CVAL341
CSER344
CARG345
CSER348
CTYR349
CTHR352
CHIS353
CARG356
CHOH710
CHOH756
CHOH771
CHOH777

site_idAE9
Number of Residues22
Detailsbinding site for residue NDP C 602
ChainResidue
CHIS185
CTYR189
CSER192
CARG194
CASN204
CTYR206
CHIS226
CLYS228
CVAL293
CTRP294
CPRO295
CHIS296
CGLN441
CALA444
CLEU445
CVAL448
CPHE449
CLYS451
CGLN455
CHOH706
CHOH740
CHOH867

site_idAF1
Number of Residues5
Detailsbinding site for residue GOL C 603
ChainResidue
BALA245
CGLY112
CALA245
CPRO249
CHOH882

site_idAF2
Number of Residues9
Detailsbinding site for residue GOL C 604
ChainResidue
CPRO376
CTHR392
CPRO393
CTYR395
CLYS396
CSER397
CCYS400
CPHE402
DTRP7

site_idAF3
Number of Residues6
Detailsbinding site for residue GOL C 605
ChainResidue
AGLY454
ACL610
CARG457
CASN458
CHIS461
CGLU496

site_idAF4
Number of Residues6
Detailsbinding site for residue GOL C 606
ChainResidue
CALA117
CARG118
CASN238
CALA241
CGLY242
CHOH791

site_idAF5
Number of Residues5
Detailsbinding site for residue GOL C 607
ChainResidue
CGLN362
CCYS368
CPRO369
CASN386
CHOH701

site_idAF6
Number of Residues4
Detailsbinding site for residue PEG C 608
ChainResidue
BLYS282
BPEG608
CGLN279
CGLN283

site_idAF7
Number of Residues6
Detailsbinding site for residue K C 609
ChainResidue
CPRO142
CGLY208
CGLN224
CLYS292
CHOH780
CHOH869

site_idAF8
Number of Residues6
Detailsbinding site for residue NA C 610
ChainResidue
CASN28
CASN34
CPRO36
CHOH815
CHOH935
CHOH976

site_idAF9
Number of Residues5
Detailsbinding site for residue K C 611
ChainResidue
CSER51
CPHE55
CHOH772
DGLN377
DMET378

site_idAG1
Number of Residues9
Detailsbinding site for residue GOL D 601
ChainResidue
AARG147
ALYS292
ATRP428
AASP438
AHOH719
AHOH786
DASN33
DALA35
DPRO36

site_idAG2
Number of Residues8
Detailsbinding site for residue GOL D 602
ChainResidue
AGLY112
AALA245
APRO249
DGLY112
DALA245
DPRO249
DHOH830
DHOH882

site_idAG3
Number of Residues9
Detailsbinding site for residue GOL D 603
ChainResidue
CHIS54
DASN360
DTHR375
DMET378
DASN386
DASN388
DLEU389
DHOH701
DHOH816

site_idAG4
Number of Residues24
Detailsbinding site for residue HEM D 604
ChainResidue
AASP56
DARG63
DVAL64
DVAL65
DHIS66
DARG103
DGLY122
DTYR138
DASN139
DPHE152
DSER207
DHIS209
DPHE325
DVAL341
DSER344
DARG345
DSER348
DTYR349
DTHR352
DHIS353
DARG356
DHOH721
DHOH744
DHOH761

site_idAG5
Number of Residues24
Detailsbinding site for residue NDP D 605
ChainResidue
DPRO142
DHIS185
DSER192
DARG194
DASN204
DTYR206
DHIS226
DLYS228
DVAL293
DTRP294
DPRO295
DHIS296
DGLN441
DALA444
DLEU445
DVAL448
DPHE449
DLYS451
DGLN455
DHOH710
DHOH723
DHOH802
DHOH880
DHOH888

site_idAG6
Number of Residues2
Detailsbinding site for residue GOL D 606
ChainResidue
BGOL605
DPHE399

site_idAG7
Number of Residues6
Detailsbinding site for residue K D 608
ChainResidue
DPRO142
DGLY208
DGLN224
DLYS292
DHOH791
DHOH834

site_idAG8
Number of Residues7
Detailsbinding site for residue NA D 609
ChainResidue
DASN28
DASN34
DALA35
DPRO36
DHOH750
DHOH954
DHOH961

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFSYpDTH
ChainResidueDetails
AARG345-HIS353

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdReripERvvHakGAG
ChainResidueDetails
APHE55-GLY71

221051

PDB entries from 2024-06-12

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