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Crystal structure of triosephosphate isomerase from brucella melitensis

Analyse Crystal structure of triosephosphate isomerase from brucella melitensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NVT
Type
protein
Length
989 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triosephosphate isomerase
EC
5.3.1.1
UniProt
C0RJA8
Pockets
8 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATriosephosphate isomerase (EC 5.3.1.1)protein24945% helix, 15% strandC0RJA8
BTriosephosphate isomerase (EC 5.3.1.1)protein24844% helix, 16% strandC0RJA8
C, DTriosephosphate isomerase (EC 5.3.1.1)protein24644% helix, 15% strandC0RJA8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19110.750.7992empty
22020.690.8744empty
31460.680.8936empty
41470.500.7926empty
51210.480.8016empty

Interfaces

5 interfaces between chains.

  • B–C · 1612 Ų buried · 34 hydrogen bonds · protein-protein
  • A–D · 1599 Ų buried · 41 hydrogen bonds · protein-protein
  • A–B · 313 Ų buried · 5 hydrogen bonds · protein-protein
  • B–D · 176 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 151 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4NVT · Crystal Structure of Triosephosphate Isomerase from Brucella melitensis · the same entry in another collection · chain A against A, TM-score 1.00

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