MolNFT v1 · #76998 · protein

Structure of bifunctional fructose 1,6-bisphosphate ALDOLASE/PHOSPHATASE (aldolase form)

3R1M · Putative uncharacterized protein ST0318: “Structure of bifunctional fructose 1,6-bisphosphate ALDOLASE/PHOSPHATASE (aldolase form)”. X-ray diffraction, 2 ligands (13P, MG), 3 pockets (best druggability 0.46). MolNFT v1 #76998 on…

PDB: 3R1M
Type: protein
Length: 356 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein ST0318
UniProt: Q975V5
Ligands: 13P, MG
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein ST0318	protein	356	28% helix, 29% strand	Q975V5

Ligands and binding sites

13P · 1,3-dihydroxyacetonephosphate · ligand · chains A
MG · Magnesium ion · metal · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.46	0.81	30	empty
2	53	0.43	0.83	13	empty
3	50	0.25	0.73	11	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3R1M · Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form) · 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 3R1M · PDBe 3R1M · UniProt Q975V5

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