9VE2: Human Peroxiredoxin I

Crystal Structure of Human Peroxiredoxin I in Complex with Fluvastatin. Determined by X-ray diffraction at 1.8 Å resolution. Released 17 Jun 2026.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,151
Mol. weight: 39.09 kDa
Ligands: 115
Released: 17 Jun 2026

Explore 9VE2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VE2 contains 17 α-helices and 22 β-strands across 2 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: 8 helices, 11 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	52-61	10
α-helix	63-68	6
β-strand	71-77	7	2
α-helix	81-89	9
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

Chain B: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	4
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	52-61	10
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	5
α-helix	121-123	3
β-strand	125-126	2	5
β-strand	128-133	6	2
β-strand	138	1	4
β-strand	139-145	7	2
α-helix	153-166	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Peroxiredoxin-1	A, B	protein	175	Homo sapiens	Q06830 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9VE2_1 Peroxiredoxin-1 (chains A, B)
MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVSPTEIIAFS
DRAEEFKKLNCQVIGASVDSHFSHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLK
ADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPA

Ligands and cofactors

ID	Name	Formula	Copies
115	(3R,5S,6E)-7-[3-(4-fluorophenyl)-1-(propan-2-yl)-1H-indol-2-yl]-3,5-dihydroxyhe…	C24 H26 F N O4	1

Primary citation

Fluvastatin protects Leydig cells in orchitis through direct activation of Peroxiredoxin 1. Zhang, H., Xu, H. To be published.

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
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
8Z55 1.83 Å, Crystal structure of human SIRT5 in complex with succPrx1 and ADP ribose

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