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Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights for its instability

Analyse Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IYN
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloroplastic ascorbate peroxidase
EC: 1.11.1.11
UniProt: Q8LNY5
Ligands: HEM, NA
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloroplastic ascorbate peroxidase (EC 1.11.1.11)	protein	275	51% helix, 3% strand	Q8LNY5

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
NA · Sodium ion · metal · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	447	0.80	0.88	52	HEM

Compared structures

1IYN · Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8LNY5
Elsewhere: RCSB PDB 1IYN · PDBe 1IYN · UniProt Q8LNY5

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