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4JB4

Expression, Purification, Characterization, and Solution NMR Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
C0004601molecular_functionperoxidase activity
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
C0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
APRO44
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ALEU232
ATHR234
AARG48
AF402
ATRP51
APRO145
AALA147
ALEU171
AMET172
AALA174
AHIS175

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE F A 402
ChainResidue
AARG48
ATRP51
AHIS52
AHEM401

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM C 401
ChainResidue
CPRO44
CARG48
CTRP51
CPRO145
CALA147
CLEU171
CMET172
CALA174
CHIS175
CGLY178
CLYS179
CTHR180
CHIS181
CASN184
CSER185
CTRP191
CLEU232
CTHR234
CF402
CHOH515

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE F C 402
ChainResidue
CARG48
CTRP51
CHIS52
CHEM401
CHOH504

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 Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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 Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
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

site_idMCSA2
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails

239803

PDB entries from 2025-08-06

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