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

4XV7

CcP gateless cavity

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 Residues22
Detailsbinding site for residue HEM A 301
ChainResidue
APRO44
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ALEU230
ATHR232
A1LQ302
AHOH474
AARG48
AHOH488
AHOH496
AHOH501
ATRP51
APRO145
AASP146
AALA147
ALEU171
AALA174
AHIS175

site_idAC2
Number of Residues9
Detailsbinding site for residue 1LQ A 302
ChainResidue
AHIS175
ALEU177
AGLY178
AGLY190
AMET228
AASP233
AHEM301
AHOH471
AHOH597

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. GPvlVRLaWHIS
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
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_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 709
ChainResidueDetails
AARG48electrostatic stabiliser
AHIS52electrostatic stabiliser, proton acceptor, proton donor

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon