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Structure of the cbs pair of a putative D-arabinose 5-phosphate isomerase from klebsiella pneumoniae subsp. pneumoniae.

Analyse Structure of the cbs pair of a putative D-arabinose 5-phosphate isomerase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3K2V
Type
protein
Length
258 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative D-arabinose 5-phosphate isomerase
UniProt
A6TEL6
Ligands
CMK, SO4
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative D-arabinose 5-phosphate isomeraseprotein13038% helix, 28% strandA6TEL6
BPutative D-arabinose 5-phosphate isomeraseprotein12838% helix, 29% strandA6TEL6

Ligands and binding sites

  • CMK · Cytidine 5'-monophosphate 3-deoxy-beta-D-gulo-oct-2-ulo-pyranosonic acid · ligand · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15520.720.8155CMK, GOL

Interfaces

1 interface between chains.

  • A–B · 1463 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

  • 3K2V · Structure of the CBS pair of a putative D-arabinose 5-phosphate isomerase from Klebsiella… · the same entry in another collection · chain A against A, TM-score 1.00

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