Research workbench

Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin biosynthesis

Analyse Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O15
Type: protein
Length: 571 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ambc
UniProt: A1YBQ4
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ambc	protein	289	21% helix, 39% strand	A1YBQ4
B	Ambc	protein	282	22% helix, 38% strand	A1YBQ4

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Pockets

6 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	233	0.74	0.88	44	empty
2	195	0.72	0.88	39	empty
3	126	0.42	0.75	34	empty
4	108	0.41	0.77	22	empty
5	66	0.40	0.80	17	empty

Interfaces

1 interface between chains.

A–B · 730 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

5O15 · Crystal structure of bifunctional dehydratase-cyclase domain in ambruticin biosynthesis · 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 A1YBQ4
Elsewhere: RCSB PDB 5O15 · PDBe 5O15 · UniProt A1YBQ4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.