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Crystal structure of the maleate isomerase iso from pseudomonas putida S16

Analyse Crystal structure of the maleate isomerase iso from pseudomonas putida S16 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4FQ7
Type
protein
Length
496 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Maleate cis-trans isomerase
UniProt
F8G0M3
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMaleate cis-trans isomeraseprotein24845% helix, 19% strandF8G0M3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13740.660.8057empty
2790.360.7614empty

Interfaces

1 interface between chains.

  • A–B · 1256 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 4FQ7 · Crystal structure of the maleate isomerase Iso from Pseudomonas putida S16 · the same entry in another collection · chain A against A, TM-score 1.00

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