Research workbench

Neisseria gonorrhoeae transaldolase, variant C38S

Analyse Neisseria gonorrhoeae transaldolase, variant C38S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BBW
Type: protein
Length: 700 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.25
Source: Neisseria gonorrhoeae
Molecule: Transaldolase
EC: 2.2.1.2
UniProt: A0A1D3FXY0
Pockets: 8 · best druggability 0.58

Structure

x-ray diffraction · resolution 1.25 · 1 distinct chain · 59% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transaldolase (EC 2.2.1.2)	protein	350	59% helix, 11% strand	A0A1D3FXY0

Ligands and binding sites

GOL · Glycerol · additive · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.58	0.78	28	GOL
2	334	0.56	0.75	48	empty
3	136	0.46	0.77	24	empty
4	113	0.43	0.77	25	empty
5	102	0.41	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 422 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7BBW · Neisseria gonorrhoeae transaldolase, variant C38S · 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 A0A1D3FXY0
Elsewhere: RCSB PDB 7BBW · PDBe 7BBW · UniProt A0A1D3FXY0

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