MolNFT v1 · #143654 · protein

Impase (AF2372) with 25 mm glutamate

6B60 · Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase: “Impase (AF2372) with 25 mm glutamate”. X-ray diffraction, 3 ligands (GLU, MG, SO4), 4 pockets (best druggability 0.69). MolNFT v1 #143654 on GenesisL1: 3D structure, binding…

PDB: 6B60
Type: protein
Length: 504 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase
EC: 3.1.3.11, 3.1.3.25
UniProt: O30298
Ligands: GLU, MG, SO4
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphatase (EC 3.1.3.11, 3.1.3.25)	protein	252	31% helix, 30% strand	O30298

Ligands and binding sites

GLU · Glutamic acid · ligand · 4 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B
SO4 · Sulfate ion · ion · 4 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	366	0.69	0.82	34	GLU, SO4, MG
2	476	0.69	0.80	48	SO4, MG, GLU
3	84	0.40	0.78	17	empty
4	80	0.30	0.73	13	empty

Interfaces

1 interface between chains.

A–B · 1228 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6B60 · IMPase (AF2372) with 25 mM Glutamate · the same entry in another collection · chain A against A, TM-score 1.00
O30298 · AlphaFold monomer V2.0 prediction for fructose-1,6-BISPHOSPHATASE/INOSITOL-1-monophosphata… · a predicted model of the same protein · chain B 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 O30298
Elsewhere: RCSB PDB 6B60 · PDBe 6B60 · UniProt O30298

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