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2IQF

Crystal structure of Helicobacter pylori catalase compound I

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
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
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 900
ChainResidue
AARG47
ATYR345
AHOH1336
BARG47
BARG344
BTYR345

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 550
ChainResidue
AVAL54
AVAL55
AHIS56
AARG93
AGLY112
AVAL127
AGLY128
AASN129
AALA139
APHE142
AGLY197
ASER198
APHE315
AMET331
AARG335
ASER338
ATYR339
ATHR342
AHIS343
AARG346
AO551
AHOH903
AHOH908
AHOH956
ALEU42
AASP46
AARG53

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE HEM B 550
ChainResidue
BLEU42
BASP46
BARG53
BVAL54
BVAL55
BHIS56
BARG93
BGLY112
BPHE113
BVAL127
BGLY128
BASN129
BALA139
BPHE142
BGLY197
BSER198
BHIS199
BPHE315
BMET331
BARG335
BSER338
BTYR339
BTHR342
BHIS343
BARG346
BO551
BHOH558
BHOH581
BHOH618

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE O A 551
ChainResidue
AVAL55
AHIS56
APHE142
AHEM550
AHOH1321

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE O B 551
ChainResidue
BHIS56
BPHE142
BHEM550
BHOH957

Functional Information from PROSITE/UniProt
site_idPS00437
Number of Residues9
DetailsCATALASE_1 Catalase proximal heme-ligand signature. RLFSYgDTH
ChainResidueDetails
AARG335-HIS343

site_idPS00438
Number of Residues17
DetailsCATALASE_2 Catalase proximal active site signature. FdReripERvvHakGSG
ChainResidueDetails
APHE45-GLY61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
ChainResidueDetails
AHIS56
AASN129
BHIS56
BASN129

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ATYR339
BTYR339

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
AHIS56
ASER95
AASN129

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1iph
ChainResidueDetails
BHIS56
BSER95
BASN129

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PDB entries from 2024-07-10

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