Research workbench

Final ketosynthase+acyltransferase of the erythromycin modular polyketide synthase

Analyse Final ketosynthase+acyltransferase of the erythromycin modular polyketide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8G4U
Type: protein
Length: 3,169 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.9
Source: Saccharopolyspora erythraea
Molecule: EryAIII
UniProt: Q5UNP4
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · resolution 2.9 · 4 distinct chains · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	EryAIII	protein	818	38% helix, 19% strand	Q5UNP4
B	EryAIII	protein	786	38% helix, 18% strand	Q5UNP4
C	EryAIII	protein	750	41% helix, 18% strand	Q5UNP4
D	EryAIII	protein	815	40% helix, 19% strand	Q5UNP4

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	609	0.75	0.82	63	empty
2	584	0.73	0.81	60	empty
3	61	0.72	0.98	23	empty
4	88	0.72	0.95	32	empty
5	52	0.72	0.99	20	empty

Interfaces

3 interfaces between chains.

C–D · 1265 Å² buried · 28 hydrogen bonds · protein-protein
A–B · 1238 Å² buried · 30 hydrogen bonds · protein-protein
B–C · 24 Å² buried · 0 hydrogen bonds · protein-protein

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 Q5UNP4
Elsewhere: RCSB PDB 8G4U · PDBe 8G4U · UniProt Q5UNP4

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