Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3TJF

Crystal Structure of human peroxiredoxin IV C51A mutant in reduced form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0007252	biological_process	I-kappaB phosphorylation
A	0007283	biological_process	spermatogenesis
A	0008379	molecular_function	thioredoxin peroxidase activity
A	0008584	biological_process	male gonad development
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0022417	biological_process	protein maturation by protein folding
A	0030198	biological_process	extracellular matrix organization
A	0034774	cellular_component	secretory granule lumen
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0042802	molecular_function	identical protein binding
A	0045454	biological_process	cell redox homeostasis
A	0051920	molecular_function	peroxiredoxin activity
A	0060090	molecular_function	molecular adaptor activity
A	0070062	cellular_component	extracellular exosome
A	0072593	biological_process	reactive oxygen species metabolic process
A	0098869	biological_process	cellular oxidant detoxification
A	0140313	molecular_function	molecular sequestering activity
A	0140824	molecular_function	thioredoxin-dependent peroxiredoxin activity
A	1904813	cellular_component	ficolin-1-rich granule lumen
A	2000255	biological_process	negative regulation of male germ cell proliferation
B	0004601	molecular_function	peroxidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0006979	biological_process	response to oxidative stress
B	0007252	biological_process	I-kappaB phosphorylation
B	0007283	biological_process	spermatogenesis
B	0008379	molecular_function	thioredoxin peroxidase activity
B	0008584	biological_process	male gonad development
B	0016209	molecular_function	antioxidant activity
B	0016491	molecular_function	oxidoreductase activity
B	0022417	biological_process	protein maturation by protein folding
B	0030198	biological_process	extracellular matrix organization
B	0034774	cellular_component	secretory granule lumen
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0042802	molecular_function	identical protein binding
B	0045454	biological_process	cell redox homeostasis
B	0051920	molecular_function	peroxiredoxin activity
B	0060090	molecular_function	molecular adaptor activity
B	0070062	cellular_component	extracellular exosome
B	0072593	biological_process	reactive oxygen species metabolic process
B	0098869	biological_process	cellular oxidant detoxification
B	0140313	molecular_function	molecular sequestering activity
B	0140824	molecular_function	thioredoxin-dependent peroxiredoxin activity
B	1904813	cellular_component	ficolin-1-rich granule lumen
B	2000255	biological_process	negative regulation of male germ cell proliferation
C	0004601	molecular_function	peroxidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005783	cellular_component	endoplasmic reticulum
C	0005829	cellular_component	cytosol
C	0006979	biological_process	response to oxidative stress
C	0007252	biological_process	I-kappaB phosphorylation
C	0007283	biological_process	spermatogenesis
C	0008379	molecular_function	thioredoxin peroxidase activity
C	0008584	biological_process	male gonad development
C	0016209	molecular_function	antioxidant activity
C	0016491	molecular_function	oxidoreductase activity
C	0022417	biological_process	protein maturation by protein folding
C	0030198	biological_process	extracellular matrix organization
C	0034774	cellular_component	secretory granule lumen
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0042802	molecular_function	identical protein binding
C	0045454	biological_process	cell redox homeostasis
C	0051920	molecular_function	peroxiredoxin activity
C	0060090	molecular_function	molecular adaptor activity
C	0070062	cellular_component	extracellular exosome
C	0072593	biological_process	reactive oxygen species metabolic process
C	0098869	biological_process	cellular oxidant detoxification
C	0140313	molecular_function	molecular sequestering activity
C	0140824	molecular_function	thioredoxin-dependent peroxiredoxin activity
C	1904813	cellular_component	ficolin-1-rich granule lumen
C	2000255	biological_process	negative regulation of male germ cell proliferation
D	0004601	molecular_function	peroxidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005829	cellular_component	cytosol
D	0006979	biological_process	response to oxidative stress
D	0007252	biological_process	I-kappaB phosphorylation
D	0007283	biological_process	spermatogenesis
D	0008379	molecular_function	thioredoxin peroxidase activity
D	0008584	biological_process	male gonad development
D	0016209	molecular_function	antioxidant activity
D	0016491	molecular_function	oxidoreductase activity
D	0022417	biological_process	protein maturation by protein folding
D	0030198	biological_process	extracellular matrix organization
D	0034774	cellular_component	secretory granule lumen
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0042802	molecular_function	identical protein binding
D	0045454	biological_process	cell redox homeostasis
D	0051920	molecular_function	peroxiredoxin activity
D	0060090	molecular_function	molecular adaptor activity
D	0070062	cellular_component	extracellular exosome
D	0072593	biological_process	reactive oxygen species metabolic process
D	0098869	biological_process	cellular oxidant detoxification
D	0140313	molecular_function	molecular sequestering activity
D	0140824	molecular_function	thioredoxin-dependent peroxiredoxin activity
D	1904813	cellular_component	ficolin-1-rich granule lumen
D	2000255	biological_process	negative regulation of male germ cell proliferation
E	0004601	molecular_function	peroxidase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
E	0005829	cellular_component	cytosol
E	0006979	biological_process	response to oxidative stress
E	0007252	biological_process	I-kappaB phosphorylation
E	0007283	biological_process	spermatogenesis
E	0008379	molecular_function	thioredoxin peroxidase activity
E	0008584	biological_process	male gonad development
E	0016209	molecular_function	antioxidant activity
E	0016491	molecular_function	oxidoreductase activity
E	0022417	biological_process	protein maturation by protein folding
E	0030198	biological_process	extracellular matrix organization
E	0034774	cellular_component	secretory granule lumen
E	0042744	biological_process	hydrogen peroxide catabolic process
E	0042802	molecular_function	identical protein binding
E	0045454	biological_process	cell redox homeostasis
E	0051920	molecular_function	peroxiredoxin activity
E	0060090	molecular_function	molecular adaptor activity
E	0070062	cellular_component	extracellular exosome
E	0072593	biological_process	reactive oxygen species metabolic process
E	0098869	biological_process	cellular oxidant detoxification
E	0140313	molecular_function	molecular sequestering activity
E	0140824	molecular_function	thioredoxin-dependent peroxiredoxin activity
E	1904813	cellular_component	ficolin-1-rich granule lumen
E	2000255	biological_process	negative regulation of male germ cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 449

Chain	Residue
A	PRO117
A	THR121
A	PHE122

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 450

Chain	Residue
A	LEU192
A	GLU193
A	ASP194
A	HOH438

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 451

Chain	Residue
A	GLU243
A	HIS241
A	GLY242

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 452

Chain	Residue
A	ASP105
A	TYR106

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 475

Chain	Residue
B	LEU192
B	GLU193
B	ASP194
B	HOH468

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 476

Chain	Residue
B	PRO117
B	THR121
B	PHE122

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 477

Chain	Residue
B	HIS241
B	GLY242

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 447

Chain	Residue
C	PRO117
C	THR121
C	PHE122

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 612

Chain	Residue
C	LEU192
C	GLU193
C	ASP194

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 448

Chain	Residue
C	HIS241
C	GLY242
C	GLU243

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 462

Chain	Residue
D	THR121
D	PHE122
D	HOH433
E	PHE154

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 463

Chain	Residue
C	LYS83
D	LEU192
D	GLU193
D	ASP194
D	SER195
D	HOH393

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 464

Chain	Residue
D	HIS241
D	GLY242
D	GLU243

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 461

Chain	Residue
E	HIS241
E	GLY242
E	GLU243

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 462

Chain	Residue
E	PRO117
E	THR121
E	PHE122

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305\|PubMed:12059788, ECO:0000305\|PubMed:21916849

Chain	Residue	Details
A	CYS124
B	CYS124
C	CYS124
D	CYS124
E	CYS124

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)