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Crystal structure of a double mutant (C202A/A198V) of triosephosphate isomerase from giardia lamblia

Analyse Crystal structure of a double mutant (C202A/A198V) of triosephosphate isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DP3
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: P36186
Ligands: SO4
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triosephosphate isomerase (EC 5.3.1.1)	protein	255	48% helix, 15% strand	P36186

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · 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	94	0.40	0.77	22	empty
2	76	0.34	0.75	26	empty

Compared structures

2DP3 · Crystal structure of a double mutant (C202A/A198V) of Triosephosphate isomerase from… · the same entry in another collection · chain A against A, TM-score 1.00
P36186 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P36186) · 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 P36186
Elsewhere: RCSB PDB 2DP3 · PDBe 2DP3 · UniProt P36186

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