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Ribokinase from leishmania donovani with ATP

Analyse Ribokinase from leishmania donovani with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A8A
Type: protein
Length: 654 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribokinase
EC: 2.7.1.15
UniProt: E9BIX7
Ligands: ATP, NA, CL
Pockets: 2 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ribokinase (EC 2.7.1.15)	protein	327	37% helix, 22% strand	E9BIX7

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 7 copies · chains A, B
CL · Chloride ion · ion · 7 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	625	0.67	0.77	66	GOL, ATP
2	559	0.67	0.77	71	ATP, CL

Interfaces

1 interface between chains.

A–B · 1367 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

6A8A · Ribokinase from Leishmania donovani with ATP · 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 E9BIX7
Elsewhere: RCSB PDB 6A8A · PDBe 6A8A · UniProt E9BIX7

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