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Crystal structure of pseudomonas malonate decarboxylase mdcd-mdce hetero-dimer

Analyse Crystal structure of pseudomonas malonate decarboxylase mdcd-mdce hetero-dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VIP
Type
protein
Length
1,009 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mdce; Mdcd
EC
2.1.3.10, 2.1.3.1
UniProt
A0A0C6EV56, A0A071KS24
Pockets
7 · best druggability 0.70

Structure

x-ray diffraction · 4 distinct chains · 44% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMdce (EC 2.1.3.10)protein25543% helix, 18% strandA0A0C6EV56
BMdcd (EC 2.1.3.10, 2.1.3.1)protein22845% helix, 20% strandA0A071KS24
CMdce (EC 2.1.3.10)protein25443% helix, 19% strandA0A0C6EV56
DMdcd (EC 2.1.3.10, 2.1.3.1)protein27244% helix, 16% strandA0A071KS24

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15700.700.7973empty
24170.660.7959empty
33720.610.7750empty
42280.520.7742empty
51680.520.7924empty

Interfaces

3 interfaces between chains.

  • C–D · 3357 Ų buried · 42 hydrogen bonds · protein-protein
  • A–B · 2979 Ų buried · 37 hydrogen bonds · protein-protein
  • B–D · 752 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 5VIP · Crystal structure of Pseudomonas malonate decarboxylase MdcD-MdcE hetero-dimer · the same entry in another collection · chain A against A, TM-score 1.00

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