Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5AL9

Structure of Leishmania major peroxidase D211R mutant (high res)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 305
ChainResidue
APRO60
AGLY195
AGLU196
ACYS197
AHIS198
APHE201
ASER202
ATRP208
ASER252
AHOH2045
AHOH2046
ASER61
AHOH2050
AHOH2054
ATRP67
APRO162
AGLY164
AVAL171
ALEU188
AALA191
AHIS192

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 307
ChainResidue
AGLU69
ASER72
ASER81
ASER86
AGLU92
AHOH2059
AHOH2060

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 310
ChainResidue
ATHR193
ATHR209
AARG211
AGLY214
ASER218
AHOH2194

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

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon