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3M5Q

0.93 A Structure of Manganese-Bound Manganese Peroxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0016689molecular_functionmanganese peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVSLLASHSV
ChainResidueDetails
AGLU165-VAL175

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AHevIRLtFHDA
ChainResidueDetails
AALA37-ALA48

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS46

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING:
ChainResidueDetails
AGLU35
ATHR193
ATHR196
AASP198
AGLU39
AASP47
AGLY62
AASP64
ASER66
ASER174
AASP179
AASP191

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS173

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG42

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN76
AASN217

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN131

227344

PDB entries from 2024-11-13

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