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5AMM

Structure of Leishmania major peroxidase D211N mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 305
ChainResidue
APRO60
AGLU196
ACYS197
AHIS198
APHE201
ASER202
ATRP208
ASER252
AHOH2006
ASER61
ATRP67
APRO162
AGLY164
ALEU188
AALA191
AHIS192
AGLY195

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 306
ChainResidue
ATHR193
ATHR209
AASN211
AGLY214
ASER218

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 308
ChainResidue
AGLU69
ASER72
AGLY80
ASER81
ASER86
AGLU92

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 305
ChainResidue
BPRO60
BSER61
BARG64
BTRP67
BPRO162
BGLY164
BLEU188
BALA191
BHIS192
BGLY195
BGLU196
BCYS197
BHIS198
BSER202
BTRP208
BSER252
BHOH2005

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 307
ChainResidue
BTHR193
BTHR209
BASN211
BGLY214

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 309
ChainResidue
BGLU69
BSER72
BSER81
BSER86
BGLU92

Functional Information from PROSITE/UniProt
site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPslIRLaWHEA
ChainResidueDetails
AGLY59-ALA70

220113

PDB entries from 2024-05-22

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