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Crystal structure of a glycerol uptake operon antiterminator-related protein (TM1436) from thermotoga maritima MSB8 at 1.65 a resolution

Analyse Crystal structure of a glycerol uptake operon antiterminator-related protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VKF
Type
protein
Length
690 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycerol uptake operon antiterminator-related protein
UniProt
Q9X1F0
Ligands
PO4
Pockets
5 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DGlycerol uptake operon antiterminator-related proteinprotein17238% helix, 25% strandQ9X1F0
B, CGlycerol uptake operon antiterminator-related proteinprotein17337% helix, 25% strandQ9X1F0

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A, B
  • CIT · Citric acid · additive · 3 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12070.590.8038PO4
22080.580.7936CIT
32280.520.7626empty
4570.350.7813CIT
5740.340.7516CIT

Interfaces

3 interfaces between chains.

  • A–B · 902 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 386 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 155 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 1VKF · Crystal structure of a glycerol uptake operon antiterminator-related protein (TM1436)… · the same entry in another collection · chain A against A, TM-score 1.00

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