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Crystal structure of transketolase mutant - H261F from pichia stipitis

Analyse Crystal structure of transketolase mutant - H261F from pichia stipitis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HGX
Type: protein
Length: 676 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transketolase
EC: 2.2.1.1
UniProt: P34736
Pockets: 4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transketolase (EC 2.2.1.1)	protein	676	45% helix, 13% strand	P34736

Ligands and binding sites

1PE · Pentaethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	275	0.59	0.78	47	empty
2	111	0.40	0.75	17	empty
3	62	0.30	0.75	14	empty
4	68	0.29	0.73	16	empty

Compared structures

5HGX · Crystal Structure of Transketolase mutant - H261F from Pichia Stipitis · the same entry in another collection · chain A against A, TM-score 1.00
P34736 · AlphaFold monomer V2.0 prediction for transketolase (P34736) · 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 P34736
Elsewhere: RCSB PDB 5HGX · PDBe 5HGX · UniProt P34736

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