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Crystal structure of mouse transaldolase

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

PDB: 2CWN
Type: protein
Length: 633 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transaldolase
EC: 2.2.1.2
UniProt: Q93092
Pockets: 5 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transaldolase (EC 2.2.1.2)	protein	321	59% helix, 12% strand	Q93092
B	Transaldolase (EC 2.2.1.2)	protein	312	57% helix, 12% strand	Q93092

Pockets

5 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	199	0.85	0.99	27	empty
2	102	0.46	0.79	22	empty
3	100	0.40	0.77	22	empty
4	63	0.30	0.74	16	empty
5	63	0.30	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 954 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2CWN · Crystal structure of mouse transaldolase · the same entry in another collection · chain A against A, TM-score 1.00
Q93092 · AlphaFold monomer V2.0 prediction for transaldolase (Q93092) · 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 Q93092
Elsewhere: RCSB PDB 2CWN · PDBe 2CWN · UniProt Q93092

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