GL1X · GenesisL1 explorer

Research workbench

Crystal structure of triosephosphate isomerase from verrucomicrobium spinosum

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

PDB
7RMN
Type
protein
Length
533 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triosephosphate isomerase
EC
5.3.1.1
Pockets
5 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATriosephosphate isomerase (EC 5.3.1.1)protein26845% helix, 14% strand—
BTriosephosphate isomerase (EC 5.3.1.1)protein26546% helix, 14% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1870.570.8720empty
2910.450.8022empty
3720.420.8017empty
4960.420.7825empty
5940.410.7820empty

Interfaces

1 interface between chains.

  • A–B · 1627 Ų buried · 31 hydrogen bonds · protein-protein

Compared structures

  • 7RMN · Crystal structure of triosephosphate isomerase from Verrucomicrobium spinosum · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.