Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XJ5

The structure of cytochrome c peroxidase Compound II

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 1295
ChainResidue
APRO44
AHIS175
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ALEU232
AVAL45
ATHR234
AHOH2171
AHOH2615
AHOH2616
AHOH2617
AARG48
ATRP51
APRO145
AASP146
ALEU171
AMET172
AALA174

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MPD A 1302
ChainResidue
ALYS59
AHIS60
AASP254
AASP256
ALYS257
ALYS260
AHOH2427
AHOH2625
AHOH2626

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1296
ChainResidue
AASP148
ASER185
ATYR187
AASN220
AHOH2618

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1297
ChainResidue
ATYR36
AASP37

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 1298
ChainResidue
ALYS12
AGLU188
AGLN222
AGLY228
ATYR229
AHOH2620

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1299
ChainResidue
ALYS97
AGLU98
AGLN240
AHOH2147
AHOH2261

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 1300
ChainResidue
ALYS264
AHOH2245
AHOH2577
AHOH2622
AHOH2623

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 1301
ChainResidue
AHOH2106

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL
ChainResidueDetails
AGLU167-LEU177

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHTS
ChainResidueDetails
AGLY43-SER54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10722697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11170452","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2169873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6092361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8384877","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8673607","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
AARG48electrostatic stabiliser
AHIS52electrostatic stabiliser, proton acceptor, proton donor
ATRP191single electron acceptor, single electron donor

244349

PDB entries from 2025-11-05

PDB statisticsPDBj update infoContact PDBjnumon