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Structure of N-terminal truncated plasmodium falciparum imp- nucleotidase

Analyse Structure of N-terminal truncated plasmodium falciparum imp- nucleotidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RN1
Type: protein
Length: 705 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Imp-specific 5'-nucleotidase, putative
EC: 3.1.3.5
UniProt: A0A144A134
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Imp-specific 5'-nucleotidase, putative (EC 3.1.3.5)	protein	358	46% helix, 15% strand	A0A144A134
B	Imp-specific 5'-nucleotidase, putative (EC 3.1.3.5)	protein	347	46% helix, 15% strand	A0A144A134

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.81	0.82	102	empty
2	161	0.78	0.94	26	empty
3	340	0.72	0.84	67	empty
4	226	0.53	0.77	33	empty
5	100	0.44	0.78	22	empty

Interfaces

1 interface between chains.

A–B · 789 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6RN1 · Structure of N-terminal truncated Plasmodium falciparum IMP-nucleotidase · 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 A0A144A134
Elsewhere: RCSB PDB 6RN1 · PDBe 6RN1 · UniProt A0A144A134

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