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Crystal structure of apo form of cyclolavandulyl diphosphate synthase (clds) from streptomyces sp. CL190

Analyse Crystal structure of apo form of cyclolavandulyl diphosphate synthase (clds)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GUK
Type: protein
Length: 432 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclolavandulyl diphosphate synthase
UniProt: X5IYJ5
Ligands: CL
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cyclolavandulyl diphosphate synthase	protein	216	49% helix, 16% strand	X5IYJ5

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	209	0.64	0.83	32	CL
2	200	0.63	0.83	31	CL
3	182	0.59	0.82	33	empty
4	207	0.58	0.81	36	empty
5	50	0.24	0.72	16	empty

Interfaces

1 interface between chains.

A–B · 1699 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5GUK · Crystal structure of apo form of cyclolavandulyl diphosphate synthase (CLDS) from… · 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
Every structure of UniProt X5IYJ5
Elsewhere: RCSB PDB 5GUK · PDBe 5GUK · UniProt X5IYJ5

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