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Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N- succinyltransferase from legionella pneumophila philadelphia 1

Analyse Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CKT
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N- succinyltransferase
EC: 2.3.1.117
UniProt: Q5ZX45
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N- succinyltransferase (EC 2.3.1.117)	protein	273	23% helix, 29% strand	Q5ZX45

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A

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

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	101	0.37	0.75	18	EDO

Compared structures

6CKT · Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
Q5ZX45 · AlphaFold monomer V2.0 prediction for 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate… · 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 Q5ZX45
Elsewhere: RCSB PDB 6CKT · PDBe 6CKT · UniProt Q5ZX45

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