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Structure of leishmania major peroxidase D211R mutant (high res)

Analyse Structure of leishmania major peroxidase D211R mutant (high res) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AL9
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ascorbate peroxidase
EC: 1.11.1.5
UniProt: Q4Q3K2
Ligands: HEM, CA, K
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ascorbate peroxidase (EC 1.11.1.5)	protein	267	51% helix, 7% strand	Q4Q3K2

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CA · Calcium ion · metal · chains A
K · Potassium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.80	0.88	52	HEM
2	52	0.26	0.73	15	empty

Compared structures

5AL9 · Structure of Leishmania major peroxidase D211R mutant (high res) · 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 Q4Q3K2
Elsewhere: RCSB PDB 5AL9 · PDBe 5AL9 · UniProt Q4Q3K2

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