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Crystal structure of tagatose-1,6-bisphosphate aldolase from streptococcus pyogenes

Analyse Crystal structure of tagatose-1,6-bisphosphate aldolase from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MYO
Type: protein
Length: 656 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tagatose 1,6-diphosphate aldolase 1
EC: 4.1.2.40
UniProt: P63703
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tagatose 1,6-diphosphate aldolase 1 (EC 4.1.2.40)	protein	328	47% helix, 16% strand	P63703

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	451	0.70	0.81	44	empty
2	461	0.69	0.80	53	empty
3	137	0.58	0.83	25	empty
4	154	0.54	0.80	26	empty
5	150	0.53	0.80	28	empty

Interfaces

1 interface between chains.

A–B · 1071 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

3MYO · Crystal structure of tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
P63703 · AlphaFold monomer V2.0 prediction for tagatose 1,6-diphosphate aldolase 1 (P63703) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P63703
Elsewhere: RCSB PDB 3MYO · PDBe 3MYO · UniProt P63703

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