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Crystal structure of riboflavin kinase from trypanosoma brucei

Analyse Crystal structure of riboflavin kinase from trypanosoma brucei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3BNW
Type
protein
Length
317 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Riboflavin kinase, putative
EC
2.7.1.26
UniProt
Q38DG4
Pockets
5 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARiboflavin kinase, putative (EC 2.7.1.26)protein16023% helix, 38% strandQ38DG4
BRiboflavin kinase, putative (EC 2.7.1.26)protein15725% helix, 38% strandQ38DG4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12500.560.7733empty
21640.450.7529empty
31030.420.7719empty
41150.400.7518empty
5900.350.7524empty

Interfaces

1 interface between chains.

  • A–B · 856 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 3BNW · Crystal structure of riboflavin kinase from Trypanosoma brucei · the same entry in another collection · chain A against A, TM-score 1.00

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