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Crystal structure of Arabidopsis thaliana cytosolic triosephosphate isomerase C13A mutant

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

PDB: 6NXQ
Type: protein
Length: 249 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.96
Source: Arabidopsis thaliana
Molecule: Triosephosphate isomerase, cytosolic
EC: 5.3.1.1
UniProt: P48491
Ligands: NA
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · resolution 1.96 · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triosephosphate isomerase, cytosolic (EC 5.3.1.1)	protein	249	44% helix, 15% strand	P48491

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.36	0.77	17	empty
2	58	0.32	0.76	17	empty

Compared structures

6NXQ · Crystal structure of arabidopsis thaliana cytosolic triosephosphate isomerase C13A mutant · the same entry in another collection · chain A against A, TM-score 1.00
P48491 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, cytosolic (P48491) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P48491
Elsewhere: RCSB PDB 6NXQ · PDBe 6NXQ · UniProt P48491

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