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Structure of the dtdp-4-keto-L-rhamnose reductase related protein (other form) from thermus thermophilus HB8

Analyse Structure of the dtdp-4-keto-L-rhamnose reductase related protein (other form)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CQ2
Type
protein
Length
386 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative uncharacterized protein TTHB138
UniProt
Q53W28
Pockets
5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, DPutative uncharacterized protein TTHB138protein9630% helix, 24% strandQ53W28
BPutative uncharacterized protein TTHB138protein9831% helix, 23% strandQ53W28

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110060.750.78101empty
2970.360.7424empty
3810.340.7522empty
4510.330.7815empty
5740.320.7413empty

Interfaces

4 interfaces between chains.

  • A–D · 597 Ų buried · 8 hydrogen bonds · protein-protein
  • A–B · 592 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 572 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 570 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 3CQ2 · Structure of the DTDP-4-Keto-L-Rhamnose Reductase related protein (other form) from… · the same entry in another collection · chain A against A, TM-score 1.00

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