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Crystal structure of Methanocaldococcus jannaschii two-subunit Fumarate hydratase apo-protein complex

Analyse Crystal structure of Methanocaldococcus jannaschii two-subunit Fumarate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7XKY
Type
protein
Length
475 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.46
Source
Methanocaldococcus jannaschii
Molecule
Fumarate hydratase
EC
4.2.1.2
UniProt
A0A832SUM4, A0A832WL32
Pockets
2 · best druggability 0.69

Structure

x-ray diffraction · resolution 2.46 · 2 distinct chains · 38% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFumarate hydratase (EC 4.2.1.2)protein28243% helix, 23% strandA0A832SUM4
BFumarate hydrataseprotein19332% helix, 31% strandA0A832WL32

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14290.690.8181empty
2620.360.7813empty

Interfaces

1 interface between chains.

  • A–B · 1265 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 modified (engineered).

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