9LG0: Human Peroxiredoxin I

Crystal Structure of Human Peroxiredoxin I in Complex with SAB. Determined by X-ray diffraction at 1.81 Å resolution. Released 1 Oct 2025.

Method: X-ray diffraction
Resolution: 1.81 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,042
Mol. weight: 39.39 kDa
Ligands: A1LXC
Released: 1 Oct 2025

Explore 9LG0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9LG0 contains 16 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	81-88	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

Chain B: 8 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
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	153-167	15

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

>9LG0_1 Peroxiredoxin-1 (chains A, B)
MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVSPTEIIAFS
DRAEEFKKLNCQVIGASVDSHFSHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLK
ADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPA

Ligands and cofactors

ID	Name	Formula	Copies
A1LXC	Salvianolic Acid B	C36 H32 O16	1

Primary citation

Augmentation of PRDX1-DOK3 interaction alleviates rheumatoid arthritis progression by suppressing plasma cell differentiation. Dang, W., Wang, X., Li, H. et al. Acta Pharm Sin B (2025) 15:3997-4013. DOI 10.1016/j.apsb.2025.06.006 · 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
8Z55 1.83 Å, Crystal structure of human SIRT5 in complex with succPrx1 and ADP ribose

Browse structure collections

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