Research workbench

Neisseria gonorrhoeae transaldolase

Analyse Neisseria gonorrhoeae transaldolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZX4
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transaldolase
EC: 2.2.1.2
UniProt: Q5F6E9
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transaldolase (EC 2.2.1.2)	protein	352	58% helix, 12% strand	Q5F6E9

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A
CIT · Citric acid · additive · chains A

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

Pockets

3 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	193	0.52	0.77	29	CIT
2	110	0.40	0.76	25	empty
3	59	0.29	0.75	14	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

6ZX4 · Neisseria gonorrhoeae transaldolase · the same entry in another collection · chain A against A, TM-score 1.00
Q5F6E9 · AlphaFold monomer V2.0 prediction for transaldolase (Q5F6E9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q5F6E9
Elsewhere: RCSB PDB 6ZX4 · PDBe 6ZX4 · UniProt Q5F6E9

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