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Crystal structure of candida glabrata FMN adenylyltransferase in complex with ATP

Analyse Crystal structure of candida glabrata FMN adenylyltransferase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3G59
Type: protein
Length: 289 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FMN adenylyltransferase
EC: 2.7.7.2
UniProt: Q6FNA9
Ligands: ATP, POP
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FMN adenylyltransferase (EC 2.7.7.2)	protein	289	40% helix, 9% strand	Q6FNA9

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
POP · Pyrophosphate 2- · ligand · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	562	0.72	0.80	41	ATP, ACT
2	105	0.48	0.80	14	empty

Compared structures

3G59 · Crystal Structure of Candida glabrata FMN Adenylyltransferase in complex with ATP · 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 Q6FNA9
Elsewhere: RCSB PDB 3G59 · PDBe 3G59 · UniProt Q6FNA9

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