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Crystal structure of ribokinase (TM0960) from thermotoga maritima at 2.15 a resolution

Analyse Crystal structure of ribokinase (TM0960) from thermotoga maritima at 2.15 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VM7
Type
protein
Length
596 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribokinase
EC
2.7.1.15
UniProt
Q9X055
Pockets
5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibokinase (EC 2.7.1.15)protein29940% helix, 24% strandQ9X055
BRibokinase (EC 2.7.1.15)protein29740% helix, 24% strandQ9X055

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16880.710.7870empty
25840.670.7771empty
3590.430.8214empty
4560.420.8214empty
5690.300.7417empty

Interfaces

1 interface between chains.

  • A–B · 1232 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 1VM7 · Crystal structure of Ribokinase (TM0960) from Thermotoga maritima at 2.15 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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