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5WHQ

Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0098869biological_processcellular oxidant detoxification
B0004096molecular_functioncatalase activity
B0004601molecular_functionperoxidase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0070301biological_processcellular response to hydrogen peroxide
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue HEM A 801
ChainResidue
AGLY83
AHIS279
ALYS283
ATHR284
AHIS285
ATHR323
ASER324
ATRP330
ALEU84
AARG87
ATRP90
AVAL239
APRO241
ALEU274
AILE275
AGLY278

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 802
ChainResidue
AGLY103
AGLU107
ASER494
AHOH908
AHOH914

site_idAC3
Number of Residues17
Detailsbinding site for residue HEM B 801
ChainResidue
BGLY83
BLEU84
BARG87
BTRP90
BLEU274
BILE275
BGLY278
BHIS279
BGLY282
BLYS283
BTHR284
BHIS285
BTHR323
BSER324
BTRP330
BTRP420
BHOH936

site_idAC4
Number of Residues4
Detailsbinding site for residue K B 802
ChainResidue
BGLU107
BSER494
BHOH911
BHOH924

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSSSGKKVSlaDL
ChainResidueDetails
AASP537-LEU549

site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHSF
ChainResidueDetails
ATHR271-PHE281

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlfIRMaWHSA
ChainResidueDetails
AGLY82-ALA93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
AHIS91
BHIS91

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
AHIS279
BHIS279

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
AARG87
BARG87

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
ATRP90
BTRP90

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-90) => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
ATYR238
AMET264
BTYR238
BMET264

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PDB entries from 2024-07-31

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