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Crystal structure of geranyltransferase from legionella pneumophila

Analyse Crystal structure of geranyltransferase from legionella pneumophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LOM
Type: protein
Length: 573 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Geranyltranstransferase
EC: 2.5.1.10
UniProt: Q5ZT35
Ligands: PO4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Geranyltranstransferase (EC 2.5.1.10)	protein	288	74% helix, 1% strand	Q5ZT35
B	Geranyltranstransferase (EC 2.5.1.10)	protein	285	76% helix, 1% strand	Q5ZT35

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	500	0.68	0.79	49	PO4
2	506	0.67	0.78	62	PO4
3	57	0.36	0.79	13	empty

Interfaces

1 interface between chains.

A–B · 1953 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

3LOM · CRYSTAL STRUCTURE OF GERANYLTRANSFERASE FROM Legionella pneumophila · 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 Q5ZT35
Elsewhere: RCSB PDB 3LOM · PDBe 3LOM · UniProt Q5ZT35

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