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Crystal structure of geranyltranstransferase (ec 2.5.1.10) (TM0161) from thermotoga maritima at 1.90 a resolution

Analyse Crystal structure of geranyltranstransferase (ec 2.5.1.10) (TM0161) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FTZ
Type: protein
Length: 265 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Geranyltranstransferase
EC: 2.5.1.10
Ligands: UNL
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 79% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Geranyltranstransferase (EC 2.5.1.10)	protein	265	79% helix, 2% strand	—

Ligands and binding sites

UNL · Unknown ligand · ligand · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 10 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	608	0.71	0.79	68	UNL, EDO
2	60	0.34	0.77	12	empty

Modifications

Observed in the structure: 24 modified (methylation).

Compared structures

2FTZ · Crystal structure of Geranyltranstransferase (EC 2.5.1.10) (tm0161) from THERMOTOGA… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 2FTZ · PDBe 2FTZ

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