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Crystal structure of sugar-phosphate aldolase from thermotoga maritima

Analyse Crystal structure of sugar-phosphate aldolase from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PVT
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sugar-phosphate aldolase
UniProt: Q9X0G1
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sugar-phosphate aldolase	protein	232	38% helix, 25% strand	Q9X0G1

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.32	0.76	15	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1PVT · Crystal structure of sugar-phosphate aldolase from Thermotoga maritima · 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 Q9X0G1
Elsewhere: RCSB PDB 1PVT · PDBe 1PVT · UniProt Q9X0G1

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