› 4jdi

X-ray diffraction
1.85Å resolution

Crystal structure of Serine/threonine-protein kinase PAK 4 in complex with Paktide S peptide substrate

Released:
DOI: 10.2210/pdb4jdi/pdb
PDB entry 4jdi coloured by chain, front view.
PDB entry 4jdi coloured by chain, side view.
PDB entry 4jdi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of a major determinant for serine-threonine kinase phosphoacceptor specificity.
Chen C, Ha BH, Thévenin AF, Lou HJ, Zhang R, Yip KY, Peterson JR, Gerstein M, Kim PM, Filippakopoulos P, Knapp S, Boggon TJ, Turk BE
Mol Cell 53 140-7 (2014)
PMID: 24374310

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132126 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PAK 4 Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 39.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O96013 (Residues: 286-591; Coverage: 52%)
Gene names: KIAA1142, PAK4
Sequence domains: Protein kinase domain
Structure domains:
Paktide S Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 1.08 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand ANP 1 x ANP
Ligand MG 2 x MG
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P41212
Unit cell:
a: 61.912Å b: 61.912Å c: 181.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.233
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Homing in: Mechanisms of Substrate Targeting by Protein Kinases.
Miller et al. (2018)
7 more

8 mentions without citation

Signaling, Regulation, and Specificity of the Type II p21-activated Kinases.
Ha et al. (2015)
7 more