› 7zx4

X-ray diffraction
2.08Å resolution

Clathrin N-terminal domain in complex with a HURP phospho-peptide

Released:
DOI: 10.2210/pdb7zx4/pdb
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PDB entry 7zx4 coloured by chain, front view.
PDB entry 7zx4 coloured by chain, side view.
PDB entry 7zx4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.
Kliche J, Garvanska DH, Simonetti L, Badgujar D, Dobritzsch D, Nilsson J, Davey NE, Ivarsson Y
OpenAccess logo Mol Syst Biol e11164 (2023)
PMID: 37219487

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-274402 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Clathrin heavy chain 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 364 amino acids
Theoretical weight: 40.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q00610 (Residues: 1-364; Coverage: 22%)
Gene names: CLH17, CLTC, CLTCL2, KIAA0034
Sequence domains:
Disks large-associated protein 5 Chains: C, D, E
Molecule details ›
Chains: C, D, E
Length: 21 amino acids
Theoretical weight: 2.46 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15398 (Residues: 826-846; Coverage: 3%)
Gene names: DLG7, DLGAP5, KIAA0008

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand CL 1 x CL
Ligand NA 1 x NA
1 modified residue:
Ligand SEP 3 x SEP

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 48.774Å b: 94.242Å c: 88.981Å
α: 90° β: 103.81° γ: 90°
R-values:
R R work R free
0.208 0.206 0.249
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

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Citations

3 review citations

The molecular basis for cellular function of intrinsically disordered protein regions.
Holehouse et al. (2024)
2 more

1 mention without citation

Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.
Kliche et al. (2023)

PDB-REDO

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