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4NFG

K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0005829cellular_componentcytosol
B0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
B0006915biological_processapoptotic process
B0008289molecular_functionlipid binding
B0009055molecular_functionelectron transfer activity
B0018063biological_processcytochrome c-heme linkage
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
B0046872molecular_functionmetal ion binding
B0070069cellular_componentcytochrome complex
B0070469cellular_componentrespirasome
B2001056biological_processpositive regulation of cysteine-type endopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 301
ChainResidue
APRO44
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ALEU232
ATHR234
AARG48
AHOH442
AHOH460
AHOH522
ATRP51
APRO145
AALA147
ALEU171
AMET172
AALA174
AHIS175

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC B 201
ChainResidue
AALA193
BARG13
BCYS14
BGLN16
BCYS17
BHIS18
BTHR28
BGLY29
BPRO30
BTHR40
BGLY41
BTYR48
BTHR49
BASN52
BTRP59
BLEU64
BTYR67
BLEU68
BTHR78
BLYS79
BMET80
BPHE82
BLEU94
BHOH346

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
DetailsBINDING: covalent
ChainResidueDetails
BCYS14
BCYS17

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:5545094
ChainResidueDetails
BHIS18

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
BMET80

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:14469771
ChainResidueDetails
BGLY1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62894
ChainResidueDetails
BTYR48
BTYR97

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
BLYS55

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
BLYS72

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
BLYS99

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

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PDB entries from 2024-07-17

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