2bgr

X-ray diffraction
2Å resolution

Crystal structure of HIV-1 Tat derived nonapeptides Tat(1-9) bound to the active site of Dipeptidyl peptidase IV (CD26)

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-146248 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (6 distinct):
Dipeptidyl peptidase 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 738 amino acids
Theoretical weight: 85.45 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P27487 (Residues: 29-766; Coverage: 96%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:
Protein Tat Chains: Y, Z
Molecule details ›
Chains: Y, Z
Length: 9 amino acids
Theoretical weight: 1.03 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: P12506 (Residues: 1-9; Coverage: 11%)
Gene name: tat

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG, FUC
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 118.299Å b: 127.043Å c: 137.332Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 0.203
Expression systems:
  • Spodoptera frugiperda
  • Not provided