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1M7S

Crystal Structure Analysis of Catalase CatF of Pseudomonas syringae

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005886cellular_componentplasma membrane
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042542biological_processresponse to hydrogen peroxide
A0042597cellular_componentperiplasmic space
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0003824molecular_functioncatalytic activity
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005737cellular_componentcytoplasm
B0005777cellular_componentperoxisome
B0005886cellular_componentplasma membrane
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042542biological_processresponse to hydrogen peroxide
B0042597cellular_componentperiplasmic space
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
C0003824molecular_functioncatalytic activity
C0004096molecular_functioncatalase activity
C0004601molecular_functionperoxidase activity
C0005737cellular_componentcytoplasm
C0005777cellular_componentperoxisome
C0005886cellular_componentplasma membrane
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
C0042542biological_processresponse to hydrogen peroxide
C0042597cellular_componentperiplasmic space
C0042744biological_processhydrogen peroxide catabolic process
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
D0003824molecular_functioncatalytic activity
D0004096molecular_functioncatalase activity
D0004601molecular_functionperoxidase activity
D0005737cellular_componentcytoplasm
D0005777cellular_componentperoxisome
D0005886cellular_componentplasma membrane
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
D0042542biological_processresponse to hydrogen peroxide
D0042597cellular_componentperiplasmic space
D0042744biological_processhydrogen peroxide catabolic process
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
AARG75
APHE163
AVAL219
AHIS220
AMET334
ALEU350
AGLY353
AARG354
ASER357
ATYR358
ATHR361
AVAL77
AGLN362
AARG365
AHOH1019
AHOH1202
AHOH1270
AHOH1673
AHOH3059
DASP68
AHIS78
AARG114
AGLY133
AVAL148
AGLY149
AASN150
APHE155

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 600
ChainResidue
BARG75
BVAL76
BVAL77
BHIS78
BARG114
BGLY133
BVAL148
BGLY149
BASN150
BPHE163
BVAL219
BHIS220
BLEU350
BGLY353
BARG354
BSER357
BTYR358
BTHR361
BGLN362
BARG365
BHOH1066
BHOH1266
BHOH1300
BHOH3125
CASP68

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM C 600
ChainResidue
BASP68
CARG75
CVAL76
CVAL77
CHIS78
CARG114
CGLY133
CVAL148
CGLY149
CASN150
CPHE155
CPHE163
CVAL219
CHIS220
CLEU350
CGLY353
CARG354
CSER357
CTYR358
CTHR361
CGLN362
CARG365
CHOH1061
CHOH1194
CHOH1335
CHOH1358

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM D 600
ChainResidue
DHOH1004
DHOH1012
DHOH1148
DHOH1242
DARG75
DVAL76
DVAL77
DHIS78
DARG114
DGLY133
DVAL148
DGLY149
DASN150
DPHE155
DPHE163
DVAL219
DHIS220
DLEU350
DGLY353
DARG354
DSER357
DTYR358
DTHR361
DGLN362
DARG365

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RVFSYaDTQ
ChainResidueDetails
AARG354-GLN362

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdReripERvvHarGTG
ChainResidueDetails
APHE67-GLY83

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
ChainResidueDetails
AHIS78
AASN150
BHIS78
BASN150
CHIS78
CASN150
DHIS78
DASN150

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ATYR358
BTYR358
CTYR358
DTYR358

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
ASER116
AASN150
AHIS78

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
BSER116
BASN150
BHIS78

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
CSER116
CASN150
CHIS78

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
DSER116
DASN150
DHIS78

219140

PDB entries from 2024-05-01

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