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Structure of the N-terminal domain of LPG1496 from legionella pneumophila in complex with nucleotide

Analyse Structure of the N-terminal domain of LPG1496 from legionella pneumophila in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BTX
Type: protein
Length: 263 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LPG1496
UniProt: G8UY02
Ligands: CMP
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LPG1496	protein	132	21% helix, 33% strand	G8UY02
B	LPG1496	protein	131	21% helix, 32% strand	G8UY02

Ligands and binding sites

CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	697	0.66	0.75	55	CMP

Interfaces

1 interface between chains.

A–B · 169 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5BTX · Structure of the N-terminal domain of lpg1496 from Legionella pneumophila in complex with… · 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 G8UY02
Elsewhere: RCSB PDB 5BTX · PDBe 5BTX · UniProt G8UY02

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