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Crystal structure of human gamma-tubulin complex protein 4 (GCP4)

Analyse Crystal structure of human gamma-tubulin complex protein 4 (GCP4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RIP
Type
protein
Length
568 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-tubulin complex component 4
UniProt
Q9UGJ1
Pockets
3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGamma-tubulin complex component 4protein56870% helix, 4% strandQ9UGJ1

Ligands and binding sites

  • GOL · Glycerol · additive · 8 copies · chains A
  • MRD · (4R)-2-methylpentane-2,4-diol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.540.8229empty
21430.480.7717empty
3850.390.7713empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3RIP · Crystal Structure of human gamma-tubulin complex protein 4 (GCP4) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UGJ1 · AlphaFold monomer V2.0 prediction for gamma-tubulin complex component 4 (Q9UGJ1) · a predicted model of the same protein · chain A against A, TM-score 0.86

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