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Crystal structure of muconolactone isomerase at 3.3 ångströms resolution

Analyse Crystal structure of muconolactone isomerase at 3.3 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1MLI
Type
protein
Length
960 residues
Chains
10
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Muconolactone isomerase
EC
5.3.3.4
UniProt
P00948

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JMuconolactone isomerase (EC 5.3.3.4)protein960% helix, 0% strandP00948

Interfaces

20 interfaces between chains.

  • A–B · 200 Ų buried · 0 hydrogen bonds · protein-protein
  • G–H · 199 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 199 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 198 Ų buried · 0 hydrogen bonds · protein-protein
  • I–J · 195 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1MLI · Crystal structure of muconolactone isomerase at 3.3 ångströms resolution · the same entry in another collection · chain J against J, TM-score 1.00
  • P00948 · AlphaFold monomer V2.0 prediction for muconolactone delta-isomerase (P00948) · a predicted model of the same protein · chain I against A, TM-score 0.92

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