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5JHZ

Crystal Structure of Fungal MagKatG2 at pH 7.0

Functional Information from GO Data
ChainGOidnamespacecontents
A0004096molecular_functioncatalase activity
A0004601molecular_functionperoxidase activity
A0005575cellular_componentcellular_component
A0005576cellular_componentextracellular region
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
B0005575cellular_componentcellular_component
B0005576cellular_componentextracellular region
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 Residues21
Detailsbinding site for residue HEM A 1500
ChainResidue
AGLY133
ALYS318
ATHR319
AHIS320
ATHR358
ASER359
ATRP365
ASER423
ATRP455
AHOH1680
AHOH1770
ALEU134
AHOH1775
AHOH1827
AVAL136
ATRP140
AVAL274
ALEU309
AGLY313
AHIS314
AGLY317

site_idAC2
Number of Residues22
Detailsbinding site for residue HEM B 1500
ChainResidue
BGLY133
BLEU134
BVAL136
BARG137
BTRP140
BVAL274
BLEU309
BGLY313
BHIS314
BGLY317
BLYS318
BTHR319
BHIS320
BTHR358
BSER359
BTRP365
BSER423
BTRP455
BHOH1658
BHOH1695
BHOH1740
BHOH1777

site_idAC3
Number of Residues21
Detailsbinding site for Di-peptide TYR B 273 and MET B 299
ChainResidue
BTRP140
BGLY144
BTHR145
BTYR146
BALA265
BALA266
BTHR267
BLEU271
BILE272
BVAL274
BALA295
BPHE296
BGLY297
BARG298
BGLY300
BMET301
BARG461
BHOH1616
BHOH1719
BHOH1969
BHOH2182

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHAF
ChainResidueDetails
ATHR306-PHE316

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GGlfVRMaWHSA
ChainResidueDetails
AGLY132-ALA143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS141
BHIS141

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS314
BHIS314

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_03108
ChainResidueDetails
AARG137
BARG137

site_idSWS_FT_FI4
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN248
BASN572
AASN302
AASN384
AASN401
AASN572
BASN248
BASN302
BASN384
BASN401

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-299)
ChainResidueDetails
ATRP140
BTRP140

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-140)
ChainResidueDetails
ATYR273
AMET299
BTYR273
BMET299

221716

PDB entries from 2024-06-26

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