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1CCG

CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND

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 Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 1
ChainResidue
APRO44
AHIS181
AASN184
ASER185
ATRP191
AHOH302
AHOH311
AHOH313
AHOH314
AIMD575
AARG48
ATRP51
AASP146
ALEU171
AALA174
AGLY178
ALYS179
ATHR180

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 575
ChainResidue
AHEM1
AMET172
AGLY175
AASP235

Functional Information from PROSITE/UniProt
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
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
AGLY175

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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