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Crystal structure of fructose-bisphosphate aldolases fbac from bacillus methanolicus

Analyse Crystal structure of fructose-bisphosphate aldolases fbac from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NC7
Type
protein
Length
545 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fructose-bisphosphate aldolase
EC
4.1.2.13
UniProt
I3EBM6
Ligands
13P
Pockets
2 · best druggability 0.48

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFructose-bisphosphate aldolase (EC 4.1.2.13)protein27351% helix, 16% strandI3EBM6
BFructose-bisphosphate aldolase (EC 4.1.2.13)protein27252% helix, 17% strandI3EBM6

Ligands and binding sites

  • 13P · 1,3-dihydroxyacetonephosphate · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11750.480.773313P
21280.440.772413P

Interfaces

1 interface between chains.

  • A–B · 1760 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 7NC7 · Crystal structure of fructose-bisphosphate aldolases FBAC from Bacillus methanolicus · the same entry in another collection · chain A against A, TM-score 1.00

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