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2GHH

Conformational mobility in the active site of a heme peroxidase

Functional Information from GO Data
ChainGOidnamespacecontents
X0000302biological_processresponse to reactive oxygen species
X0004601molecular_functionperoxidase activity
X0006979biological_processresponse to oxidative stress
X0009507cellular_componentchloroplast
X0016688molecular_functionL-ascorbate peroxidase activity
X0020037molecular_functionheme binding
X0034599biological_processcellular response to oxidative stress
X0042744biological_processhydrogen peroxide catabolic process
X0046872molecular_functionmetal ion binding
X0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K X 9252
ChainResidue
XTHR164
XTHR180
XASN182
XILE185
XASP187

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM X 251
ChainResidue
XPHE145
XLEU159
XGLY162
XHIS163
XILE165
XGLY166
XALA167
XALA168
XHIS169
XARG172
XSER173
XTRP179
XLEU205
XSER207
XTYR235
XNO9260
XHOH9269
XHOH9287
XHOH9302
XHOH9379
XPRO34
XTRP41
XPRO132
XALA134

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO X 9260
ChainResidue
XARG38
XTRP41
XHIS42
XHEM251
XHOH9299
XHOH9379

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIVALSGGHTI
ChainResidueDetails
XASP155-ILE165

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. APlmLRLaWHSA
ChainResidueDetails
XALA33-ALA44

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PDB entries from 2024-06-05

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