MolNFT v1 · #24165 · protein

Crystal structure of fructose-1,6-bisphosphatase

1UMG · 385AA long conserved hypothetical protein: “Crystal structure of fructose-1,6-bisphosphatase”. X-ray diffraction, 2 ligands (2FP, MG), 3 pockets (best druggability 0.76). MolNFT v1 #24165 on GenesisL1: 3D structure, binding sites…

PDB: 1UMG
Type: protein
Length: 359 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 385AA long conserved hypothetical protein
EC: 3.1.3.11
UniProt: Q975V5
Ligands: 2FP, MG
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	385AA long conserved hypothetical protein (EC 3.1.3.11)	protein	359	29% helix, 29% strand	Q975V5

Ligands and binding sites

2FP · 1,6-fructose diphosphate (linear form) · ligand · chains A
MG · Magnesium ion · metal · 4 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

3 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	312	0.76	0.88	54	MG, 2FP
2	103	0.41	0.76	20	empty
3	56	0.30	0.75	15	empty

Compared structures

1UMG · Crystal structure of fructose-1,6-bisphosphatase · 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 Q975V5
Elsewhere: RCSB PDB 1UMG · PDBe 1UMG · UniProt Q975V5

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