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Structure of yeast triosephosphate isomerase at 1.9- ångströms resolution

Analyse Structure of yeast triosephosphate isomerase at 1.9- ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YPI
Type: protein
Length: 494 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: P00942
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Triosephosphate isomerase (EC 5.3.1.1)	protein	247	43% helix, 17% strand	P00942

Pockets

3 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	124	0.46	0.78	27	empty
2	156	0.45	0.76	36	empty
3	52	0.29	0.76	18	empty

Interfaces

1 interface between chains.

A–B · 1682 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

1YPI · Structure of yeast triosephosphate isomerase at 1.9-ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
P00942 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase (P00942) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P00942
Elsewhere: RCSB PDB 1YPI · PDBe 1YPI · UniProt P00942

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