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1QQ2

CRYSTAL STRUCTURE OF A MAMMALIAN 2-CYS PEROXIREDOXIN, HBP23.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0000791cellular_componenteuchromatin
A0004601molecular_functionperoxidase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0007249biological_processcanonical NF-kappaB signal transduction
A0008379molecular_functionthioredoxin peroxidase activity
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0020037molecular_functionheme binding
A0030101biological_processnatural killer cell activation
A0032872biological_processregulation of stress-activated MAPK cascade
A0034101biological_processerythrocyte homeostasis
A0042267biological_processnatural killer cell mediated cytotoxicity
A0042744biological_processhydrogen peroxide catabolic process
A0042802molecular_functionidentical protein binding
A0045321biological_processleukocyte activation
A0045454biological_processcell redox homeostasis
A0048144biological_processfibroblast proliferation
A0050896biological_processresponse to stimulus
A0051920molecular_functionperoxiredoxin activity
A0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
A1901222biological_processregulation of non-canonical NF-kappaB signal transduction
B0000302biological_processresponse to reactive oxygen species
B0000791cellular_componenteuchromatin
B0004601molecular_functionperoxidase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005759cellular_componentmitochondrial matrix
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0007249biological_processcanonical NF-kappaB signal transduction
B0008379molecular_functionthioredoxin peroxidase activity
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0020037molecular_functionheme binding
B0030101biological_processnatural killer cell activation
B0032872biological_processregulation of stress-activated MAPK cascade
B0034101biological_processerythrocyte homeostasis
B0042267biological_processnatural killer cell mediated cytotoxicity
B0042744biological_processhydrogen peroxide catabolic process
B0042802molecular_functionidentical protein binding
B0045321biological_processleukocyte activation
B0045454biological_processcell redox homeostasis
B0048144biological_processfibroblast proliferation
B0050896biological_processresponse to stimulus
B0051920molecular_functionperoxiredoxin activity
B0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
B1901222biological_processregulation of non-canonical NF-kappaB signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
AGLU55
AARG128
AHOH252

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BGLU55
BARG128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Cysteine sulfenic acid (-SOH) intermediate
ChainResidueDetails
ACYS52
BCYS52

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ALYS7
BLYS7

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ALYS16
ALYS27
BLYS16
BLYS27

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ASER32
BSER32

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P35700
ChainResidueDetails
ALYS35
BLYS35

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ATHR90
BTHR90

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P35700
ChainResidueDetails
ALYS136
BLYS136

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ALYS7
BLYS7

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ALYS185
BLYS185

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q06830
ChainResidueDetails
ALYS120
BLYS120

218853

PDB entries from 2024-04-24

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