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4MH2

Crystal structure of Bovine Mitochondrial Peroxiredoxin III

Functional Information from GO Data
ChainGOidnamespacecontents
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0051920molecular_functionperoxiredoxin activity
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0051920molecular_functionperoxiredoxin activity
C0016209molecular_functionantioxidant activity
C0016491molecular_functionoxidoreductase activity
C0051920molecular_functionperoxiredoxin activity
D0016209molecular_functionantioxidant activity
D0016491molecular_functionoxidoreductase activity
D0051920molecular_functionperoxiredoxin activity
E0016209molecular_functionantioxidant activity
E0016491molecular_functionoxidoreductase activity
E0051920molecular_functionperoxiredoxin activity
F0016209molecular_functionantioxidant activity
F0016491molecular_functionoxidoreductase activity
F0051920molecular_functionperoxiredoxin activity
G0016209molecular_functionantioxidant activity
G0016491molecular_functionoxidoreductase activity
G0051920molecular_functionperoxiredoxin activity
H0016209molecular_functionantioxidant activity
H0016491molecular_functionoxidoreductase activity
H0051920molecular_functionperoxiredoxin activity
I0016209molecular_functionantioxidant activity
I0016491molecular_functionoxidoreductase activity
I0051920molecular_functionperoxiredoxin activity
J0016209molecular_functionantioxidant activity
J0016491molecular_functionoxidoreductase activity
J0051920molecular_functionperoxiredoxin activity
K0016209molecular_functionantioxidant activity
K0016491molecular_functionoxidoreductase activity
K0051920molecular_functionperoxiredoxin activity
L0016209molecular_functionantioxidant activity
L0016491molecular_functionoxidoreductase activity
L0051920molecular_functionperoxiredoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 201
ChainResidue
AHIS136
BTHR151
ASER138
AARG146
AGLU150
AHOH377
BHIS136
BSER138
BARG146
BGLU150

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CIT D 201
ChainResidue
CHIS136
CSER138
CARG146
CSER147
CGLU150
CTHR151
CHOH227
DHIS136
DSER138
DARG146
DSER147
DGLU150
DTHR151
DLEU154

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT F 201
ChainResidue
EHIS136
ESER138
ETHR151
ELEU154
FHIS136
FSER138
FARG146
FSER147
FGLU150
FTHR151

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT H 201
ChainResidue
GHIS136
GSER138
GARG146
GSER147
GTHR151
HHIS136
HSER138
HARG146
HGLU150
HTHR151

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT J 201
ChainResidue
IHIS136
ISER138
IARG146
ISER147
ITHR151
JHIS136
JSER138
JSER147
JGLU150
JTHR151

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT L 201
ChainResidue
KHIS136
KARG146
KGLU150
LHIS136
LSER138
LASN140
LARG146
LSER147
LGLU150
LTHR151
LHOH320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000269|PubMed:8089078
ChainResidueDetails
ACYS47
JCYS47
KCYS47
LCYS47
BCYS47
CCYS47
DCYS47
ECYS47
FCYS47
GCYS47
HCYS47
ICYS47

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20108
ChainResidueDetails
ALYS22
JLYS22
KLYS22
LLYS22
BLYS22
CLYS22
DLYS22
ELYS22
FLYS22
GLYS22
HLYS22
ILYS22

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P20108
ChainResidueDetails
ALYS30
JLYS30
KLYS30
LLYS30
BLYS30
CLYS30
DLYS30
ELYS30
FLYS30
GLYS30
HLYS30
ILYS30

site_idSWS_FT_FI4
Number of Residues12
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P30048
ChainResidueDetails
ATHR85
JTHR85
KTHR85
LTHR85
BTHR85
CTHR85
DTHR85
ETHR85
FTHR85
GTHR85
HTHR85
ITHR85

223790

PDB entries from 2024-08-14

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