› 1b89

X-ray diffraction
2.6Å resolution

CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)

Released:
DOI: 10.2210/pdb1b89/pdb
PDB entry 1b89 coloured by chain, front view.
PDB entry 1b89 coloured by chain, side view.
PDB entry 1b89 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Clathrin self-assembly is mediated by a tandemly repeated superhelix.
Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK
Nature 399 371-5 (1999)
PMID: 10360576

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156099 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Clathrin heavy chain 1 Chain: A
Molecule details ›
Chain: A
Length: 449 amino acids
Theoretical weight: 52.68 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49951 (Residues: 1074-1522; Coverage: 27%)
Gene name: CLTC
Sequence domains: Region in Clathrin and VPS
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: I4122
Unit cell:
a: 145.2Å b: 145.2Å c: 166.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.254 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Biological basket weaving: formation and function of clathrin-coated vesicles.
Brodsky et al. (2001)
25 more

9 mentions without citation

Components of coated vesicles and nuclear pore complexes share a common molecular architecture.
Devos et al. (2004)
8 more