3HY2: Sulfiredoxin

Crystal Structure of Sulfiredoxin in Complex with Peroxiredoxin I and ATP:Mg2+. Determined by X-ray diffraction at 2.1 Å resolution. Released 6 Oct 2009.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,835
Mol. weight: 71.17 kDa
Ligands: ATP, MG
Released: 6 Oct 2009

Explore 3HY2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HY2 contains 33 α-helices and 34 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
α-helix	12-14	3
β-strand	16-20	5	2
β-strand	26-30	5	2
α-helix	31-34	4
β-strand	38-43	6	2
α-helix	54-61	8
α-helix	63-68	6
β-strand	71-77	7	2
α-helix	81-88	8
α-helix	92-94	3
β-strand	104-106	3	2
α-helix	111-115	5
β-strand	119-120	2	3
β-strand	125-126	2	3
β-strand	128-133	6	2
β-strand	138	1	1
β-strand	139-145	7	2
α-helix	153-168	16
α-helix	181-183	3
β-strand	184	1	4
α-helix	185-186	2

Chain B: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	5
α-helix	12-14	3
β-strand	16-20	5	2
β-strand	26-30	5	2
α-helix	31-34	4
β-strand	38-43	6	2
α-helix	54-61	8
α-helix	63-67	5
β-strand	71-77	7	2
α-helix	81-88	8
α-helix	92-94	3
β-strand	104-106	3	2
α-helix	111-115	5
β-strand	119-120	2	6
β-strand	125-126	2	6
β-strand	128-133	6	2
β-strand	138	1	5
β-strand	139-145	7	2
α-helix	153-168	16
α-helix	181-183	3
β-strand	184	1	7

Chains X and Y: 7 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	42-45	4	7
α-helix	46-48	3
β-strand	49-50	2	7
α-helix	59-71	13
α-helix	73-75	3
α-helix	77-78	2
β-strand	79-85	7	7
β-strand	91-95	5	7
α-helix	99-107	9
β-strand	112-120	9	7
α-helix	122-129	8
α-helix	130-132	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peroxiredoxin-1	A, B	protein	206	Homo sapiens	Q06830 (AlphaFold model)
Sulfiredoxin-1	X, Y	protein	110	Homo sapiens	Q9BYN0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3HY2_1 Peroxiredoxin-1 (chains A, B)
MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVDPTEIIAFS
DRAEEFKKLNSQVIGASVDSHFEHLEWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLK
ADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVSPAGWKPG
SDTICPDVQKSKEYFSKQKGHHHHHH

Sequence of entity 2 (X, Y), FASTA

>3HY2_2 Sulfiredoxin-1 (chains X, Y)
GHPMSIHSGRIAAVHCVPLSVLIRPLPSVLDPAKVQSLVDTIREDPDSVPPIDVLWIKGA
QGGDYFYSFGGAHRYAAYQQLQRETIPAKLVQSTLSDLRVYLGASTPDLQ

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

Protein Engineering of the Quaternary Sulfiredoxin-Peroxiredoxin Enzyme-Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation. Jonsson, T.J., Johnson, L.C., Lowther, W.T. J Biol Chem (2009) 284:33305-33310. DOI 10.1074/jbc.M109.036400 · PubMed

Other PDB entries of the same protein (UniProt Q06830 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8Z54 1.45 Å, Crystal structure of human SIRT5 in complex with succinylated Prx1 fragment
9VQ5 1.5 Å, Crystal structure of Peroxiredoxin I in complex with SAC
8X71 1.58 Å, Crystal structure of Peroxiredoxin I in complex with compound 19-064
8X73 1.61 Å, Crystal structure of Peroxiredoxin I in complex with compound 19-069
9LNH 1.63 Å, Crystal structure of Peroxiredoxin I in complex with compound LC-PDin20
9B7A 1.71 Å, Crystal structure of peroxiredoxin 1 with RA
7WET 1.76 Å, Crystal structure of Peroxiredoxin I in complex with the inhibitor Cela
9VGT 1.79 Å, Crystal structure of Peroxiredoxin I in complex with compound 19-150
9VE2 1.8 Å, Crystal Structure of Human Peroxiredoxin I in Complex with Fluvastatin
8Z56 1.81 Å, Crystal structure of human Q140L-SIRT5 in complex with succinylated Prx1 fragment
7WEU 1.81 Å, Crystal structure of Peroxiredoxin I in complex with compound 19-048
9LG0 1.81 Å, Crystal Structure of Human Peroxiredoxin I in Complex with SAB

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