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Crystal structure of lactococcus lactis pyruvate carboxylase

Analyse Crystal structure of lactococcus lactis pyruvate carboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VYW
Type
protein
Length
3,984 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pyruvate carboxylase
EC
6.4.1.1
UniProt
A0A089XIW4
Ligands
BTN, MN
Pockets
20 · best druggability 0.84

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
APyruvate carboxylase (EC 6.4.1.1)protein98144% helix, 18% strandA0A089XIW4
BPyruvate carboxylase (EC 6.4.1.1)protein97944% helix, 18% strandA0A089XIW4
CPyruvate carboxylase (EC 6.4.1.1)protein97844% helix, 18% strandA0A089XIW4
DPyruvate carboxylase (EC 6.4.1.1)protein104643% helix, 18% strandA0A089XIW4

Ligands and binding sites

  • BTN · Biotin · ligand · chains A
  • MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111490.840.85117empty
26020.820.8882empty
310530.810.83133MN
43830.780.8862empty
59460.780.80108MN

Interfaces

4 interfaces between chains.

  • B–C · 3021 Ų buried · 63 hydrogen bonds · protein-protein
  • A–D · 2936 Ų buried · 57 hydrogen bonds · protein-protein
  • A–C · 1688 Ų buried · 19 hydrogen bonds · protein-protein
  • B–D · 1655 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 5VYW · Crystal structure of Lactococcus lactis pyruvate carboxylase · the same entry in another collection · chain A against A, TM-score 1.00

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