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Crystal structure of the LIN1889 protein (Q92AN1) from listeria innocua. northeast structural consortium target LKR65

Analyse Crystal structure of the LIN1889 protein (Q92AN1) from listeria innocua.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B57
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LIN1889 protein
UniProt: Q92AN1
Ligands: MG
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LIN1889 protein	protein	180	71% helix, 0% strand	Q92AN1

Ligands and binding sites

MG · Magnesium ion · metal · 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	112	0.37	0.74	23	MG

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

3B57 · Crystal structure of the Lin1889 protein (Q92AN1) from Listeria innocua. Northeast… · 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 Q92AN1
Elsewhere: RCSB PDB 3B57 · PDBe 3B57 · UniProt Q92AN1

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