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Crystal structure of escherichia COLI transaldolase B mutant D17A

Analyse Crystal structure of escherichia COLI transaldolase B mutant D17A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1I2P
Type: protein
Length: 632 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transaldolase B
EC: 2.2.1.2
UniProt: P0A870
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transaldolase B (EC 2.2.1.2)	protein	316	56% helix, 13% strand	P0A870

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.82	0.97	27	empty
2	150	0.51	0.79	24	empty
3	144	0.51	0.79	24	empty

Interfaces

1 interface between chains.

A–B · 832 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1I2P · Crystal structure of escherichia COLI transaldolase B mutant D17A · the same entry in another collection · chain A against A, TM-score 1.00
P0A870 · AlphaFold monomer V2.0 prediction for transaldolase B (P0A870) · 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 P0A870
Elsewhere: RCSB PDB 1I2P · PDBe 1I2P · UniProt P0A870

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