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2V2E

Structure of isoniazid (INH) bound to cytochrome c peroxidase mutant N184R Y36A

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 Residues25
DetailsBINDING SITE FOR RESIDUE HEM A1295
ChainResidue
APRO44
AHIS175
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AARG184
ASER185
ATRP191
ALEU232
AARG48
ATHR234
AISZ1296
AHOH2063
AHOH2312
AHOH2313
AHOH2314
ATRP51
APRO145
AASP146
AALA147
ALEU171
AMET172
AALA174

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ISZ A1296
ChainResidue
AARG48
AHIS52
APRO145
AHEM1295
AHOH2063
AHOH2208

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS52

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate
ChainResidueDetails
ATRP191

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS175

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG48

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATYR153

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 2024-05-01

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