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Crystal structure of E. COLI fumarase C bound to citrate at 1.53 ångström resolution

Analyse Crystal structure of E. COLI fumarase C bound to citrate at 1.53 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6NZ9
Type
protein
Length
915 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fumarate hydratase class II
EC
4.2.1.2
UniProt
P05042
Pockets
5 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFumarate hydratase class II (EC 4.2.1.2)protein45662% helix, 8% strandP05042
BFumarate hydratase class II (EC 4.2.1.2)protein45962% helix, 8% strandP05042

Ligands and binding sites

  • CIT · Citric acid · additive · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13380.530.7437empty
22110.440.7326empty
3930.360.7519empty
4630.310.7512empty
5540.300.7518empty

Interfaces

1 interface between chains.

  • A–B · 2889 Ų buried · 38 hydrogen bonds · protein-protein

Compared structures

  • 6NZ9 · Crystal structure of E. coli fumarase C bound to citrate at 1.53 angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • P05042 · AlphaFold monomer V2.0 prediction for fumarate hydratase class II (P05042) · a predicted model of the same protein · chain B against A, TM-score 0.97

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