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Structure of a prenyltransferase in its unbound form

Analyse Structure of a prenyltransferase in its unbound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5B01
Type: protein
Length: 2,620 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MOEN5
UniProt: A0A010
Pockets: 16 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	MOEN5	protein	262	78% helix, 0% strand	A0A010

Pockets

16 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	668	0.78	0.83	66	empty
2	643	0.78	0.83	63	empty
3	694	0.78	0.82	64	empty
4	666	0.77	0.82	64	empty
5	655	0.77	0.82	62	empty

Interfaces

10 interfaces between chains.

A–B · 1775 Å² buried · 23 hydrogen bonds · protein-protein
E–F · 1759 Å² buried · 25 hydrogen bonds · protein-protein
C–D · 1749 Å² buried · 26 hydrogen bonds · protein-protein
I–J · 1730 Å² buried · 21 hydrogen bonds · protein-protein
G–H · 1725 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5B01 · Structure of a prenyltransferase in its unbound form · 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 A0A010
Elsewhere: RCSB PDB 5B01 · PDBe 5B01 · UniProt A0A010

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