1APX: Recombinant ascorbate peroxidase

Crystal structure of recombinant ascorbate peroxidase. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Mar 1996.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Pisum sativum
Chains
4
Atoms
8,481
Mol. weight
111.01 kDa
Ligands
HEM
Released
8 Mar 1996

Explore 1APX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1APX contains 75 α-helices and 16 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: 18 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix5-95
α-helix10-3021
α-helix33-4412
β-strand4811
β-strand5311
α-helix59-613
α-helix63-664
α-helix69-713
α-helix74-8613
α-helix93-10715
α-helix125-1273
α-helix132-1332
α-helix138-1414
α-helix142-1487
α-helix153-1608
α-helix161-1644
β-strand167-16822
β-strand177-17822
α-helix189-1957
α-helix206-2094
α-helix217-22610
α-helix228-24316
Chain B: 20 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix5-73
α-helix10-3021
α-helix33-4412
β-strand4813
β-strand5313
α-helix59-613
α-helix63-664
α-helix69-713
α-helix74-8512
α-helix93-10715
α-helix119-1213
α-helix125-1273
α-helix138-1425
α-helix143-1497
α-helix153-1608
α-helix161-1644
β-strand167-16824
α-helix170-1734
β-strand177-17824
α-helix189-1957
α-helix206-2094
α-helix210-2134
α-helix217-22610
α-helix228-24316
Chain C: 18 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix10-3021
α-helix33-4412
β-strand4815
β-strand5315
α-helix59-613
α-helix63-664
α-helix69-713
α-helix74-8512
α-helix93-10715
α-helix125-1273
α-helix132-1332
α-helix138-1414
α-helix142-1487
α-helix153-1608
α-helix161-1644
β-strand167-16826
α-helix170-1734
β-strand177-17826
α-helix189-1957
α-helix206-2094
α-helix217-22610
α-helix228-24316
Chain D: 19 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix10-3021
α-helix33-4412
β-strand4817
β-strand5317
α-helix59-613
α-helix63-664
α-helix69-713
α-helix74-8512
α-helix93-10715
α-helix125-1273
α-helix132-1332
α-helix138-1414
α-helix142-1498
α-helix153-1608
α-helix161-1644
β-strand167-16828
α-helix170-1734
β-strand177-17828
α-helix189-1957
α-helix206-2094
α-helix210-2134
α-helix217-22610
α-helix228-24316

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytosolic ascorbate peroxidaseA, B, C, Dprotein249Pisum sativumP48534 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1APX_1 CYTOSOLIC ASCORBATE PEROXIDASE (chains A, B, C, D)
GKSYPTVSPDYQKAIEKAKRKLRGFIAEKKCAPLILRLAWHSAGTFDSKTKTGGPFGTIK
HQAELAHGANNGLDIAVRLLEPIKEQFPIVSYADFYQLAGVVAVEITGGPEVPFHPGRED
KPEPPPEGRLPDATKGSDHLRDVFGKAMGLSDQDIVALSGGHTIGAAHKERSGFEGPWTS
NPLIFDNSYFTELLTGEKDGLLQLPSDKALLTDSVFRPLVEKYAADEDVFFADYAEAHLK
LSELGFAEA

Ligands and cofactors

IDNameFormulaCopies
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O44

Water and common crystallization additives (K) are not listed.

Primary citation

Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Patterson, W.R., Poulos, T.L. Biochemistry (1995) 34:4331-4341. DOI 10.1021/bi00013a023 · PubMed

Other PDB entries of the same protein (UniProt P48534 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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