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Human tubulin chaperone cofactor a

Analyse Human tubulin chaperone cofactor a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1H7C
Type
protein
Length
103 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tubulin-specific chaperone a
UniProt
O75347
Ligands
SO4

Structure

x-ray diffraction · 1 distinct chain · 88% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATubulin-specific chaperone aprotein10388% helix, 0% strandO75347

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • ACY · Acetic acid · additive · chains A

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

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 1H7C · human tubulin chaperone cofactor a · the same entry in another collection · chain A against A, TM-score 1.00
  • O75347 · AlphaFold monomer V2.0 prediction for tubulin-specific chaperone a (O75347) · a predicted model of the same protein · chain A against A, TM-score 0.92

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