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Crystal structure of muconate cycloisomerase from pseudomonas fluorescens

Analyse Crystal structure of muconate cycloisomerase from pseudomonas fluorescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CT2
Type
protein
Length
722 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Muconate cycloisomerase
EC
5.5.1.1
UniProt
Q4K9X1
Ligands
MG
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BMuconate cycloisomerase (EC 5.5.1.1)protein36142% helix, 21% strandQ4K9X1

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17760.780.8274empty
21820.550.7944empty
31480.530.8031empty

Interfaces

1 interface between chains.

  • A–B · 1285 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 3CT2 · Crystal structure of muconate cycloisomerase from Pseudomonas fluorescens · the same entry in another collection · chain B against B, TM-score 1.00

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