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Membrane-bound glutamate carboxypeptidase II (gcpii) with bound glutamate

Analyse Membrane-bound glutamate carboxypeptidase II (gcpii) with bound glutamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C6G
Type
protein
Length
679 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glutamate carboxypeptidase II
EC
3.4.17.21
UniProt
Q04609
Ligands
GLU, NAG, BMA, MAN, ZN, CA, CL
Pockets
7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlutamate carboxypeptidase II (EC 3.4.17.21)protein67939% helix, 19% strandQ04609

Ligands and binding sites

  • GLU · Glutamic acid · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A
  • BMA · beta-D-mannopyranose · sugar
  • MAN · alpha-D-mannopyranose · sugar
  • ZN · Zinc ion · metal · 2 copies · chains A
  • CA · Calcium ion · metal · chains A
  • CL · Chloride ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14160.720.8358GLU, CL
23210.550.7553empty
31850.480.7519empty
41160.420.7626empty
5860.320.7320empty

Modifications

Observed in the structure: 6 glycan (N-glycosylation).

Compared structures

  • 2C6G · Membrane-bound glutamate carboxypeptidase II (GCPII) with bound glutamate · the same entry in another collection · chain A against A, TM-score 1.00
  • Q04609 · AlphaFold monomer V2.0 prediction for glutamate carboxypeptidase 2 (Q04609) · a predicted model of the same protein · chain A against A, TM-score 1.00

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