MolNFT v1 · #91383 · protein

Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6- phosphate complex (R form)

4FBP · Fructose 1,6-bisphosphatase: “Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T…”. X-ray diffraction, 1 ligand (AMP), 18 pockets (best druggability 0.83). MolNFT v1 #91383 on…

PDB: 4FBP
Type: protein
Length: 1,268 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose 1,6-bisphosphatase
EC: 3.1.3.11
UniProt: P00636
Ligands: AMP
Pockets: 18 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Fructose 1,6-bisphosphatase (EC 3.1.3.11)	protein	317	39% helix, 25% strand	P00636

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · 4 copies · chains A, B, D, C

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

Pockets

18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1068	0.83	0.83	98	empty
2	59	0.69	0.97	27	empty
3	221	0.57	0.79	40	empty
4	234	0.55	0.78	36	empty
5	149	0.54	0.81	26	empty

Interfaces

6 interfaces between chains.

C–D · 2288 Å² buried · 30 hydrogen bonds · protein-protein
A–B · 2257 Å² buried · 29 hydrogen bonds · protein-protein
A–C · 1184 Å² buried · 18 hydrogen bonds · protein-protein
B–D · 1112 Å² buried · 15 hydrogen bonds · protein-protein
A–D · 404 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

4FBP · Conformational transition of fructose-1,6-bisphosphatase: structure comparison between… · the same entry in another collection · chain D against D, TM-score 1.00
P00636 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P00636) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P00636
Elsewhere: RCSB PDB 4FBP · PDBe 4FBP · UniProt P00636

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