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Guanosine Monophosphate Synthase from Aspergillus fumigatus Af293

Analyse Guanosine Monophosphate Synthase from Aspergillus fumigatus Af293 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MO6
Type: protein
Length: 1,053 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: Aspergillus fumigatus Af293
Molecule: GMP synthase [glutamine-hydrolyzing]
EC: 6.3.5.2
UniProt: A0A229XUE6
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · resolution 2.3 · 2 distinct chains · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)	protein	518	35% helix, 22% strand	A0A229XUE6
B	GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2)	protein	535	38% helix, 23% strand	A0A229XUE6

Pockets

7 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	997	0.73	0.76	93	empty
2	905	0.72	0.77	80	empty
3	755	0.68	0.76	73	empty
4	176	0.50	0.78	21	empty
5	103	0.44	0.79	18	empty

Interfaces

1 interface between chains.

A–B · 360 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7MO6 · Guanosine monophosphate synthase from aspergillus fumigatus AF293 · 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 A0A229XUE6
Elsewhere: RCSB PDB 7MO6 · PDBe 7MO6 · UniProt A0A229XUE6

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