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Crystal structure of P. falciparum arginase complexed with 2-amino-6- borono-2-methylhexanoic acid

Analyse Crystal structure of P. falciparum arginase complexed with 2-amino-6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SL1
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginase
EC: 3.5.3.1
UniProt: Q8I384
Ligands: FB6, MN
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Arginase (EC 3.5.3.1)	protein	308	41% helix, 17% strand	Q8I384

Ligands and binding sites

FB6 · 6-(dihydroxyboranyl)-2-methyl-L-norleucine · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	96	0.45	0.80	24	FB6
2	93	0.45	0.79	17	empty
3	56	0.34	0.78	17	empty

Compared structures

3SL1 · Crystal Structure of P. falciparum arginase complexed with… · 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 Q8I384
Elsewhere: RCSB PDB 3SL1 · PDBe 3SL1 · UniProt Q8I384

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