MolNFT v1 · #118339 · protein

Crystal structure of litopenaeus vannamei triosephosphate isomerase complexed with 2-phosphoglycolic acid

5EYW: “Crystal structure of litopenaeus vannamei triosephosphate isomerase complexed with 2-phosphoglycolic acid”. X-ray diffraction, 1 ligand (PGA), 1 pocket (best druggability 0.35). MolNFT v1 #118339 on GenesisL1: 3D structure, binding…

PDB: 5EYW
Type: protein
Length: 488 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triosephosphate isomerase
EC: 5.3.1.1
UniProt: K0E682
Ligands: PGA
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Triosephosphate isomerase (EC 5.3.1.1)	protein	244	46% helix, 17% strand	K0E682

Ligands and binding sites

PGA · 2-phosphoglycolic acid · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.35	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 1657 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

5EYW · Crystal structure of Litopenaeus vannamei triosephosphate isomerase complexed with… · the same entry in another collection · 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 K0E682
Elsewhere: RCSB PDB 5EYW · PDBe 5EYW · UniProt K0E682

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