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› 1clw

X-ray diffraction
2Å resolution

TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT

Released:
DOI: 10.2210/pdb1clw/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1clw coloured by chain, front view.
PDB entry 1clw coloured by chain, side view.
PDB entry 1clw coloured by chain, top view.
Source organism: Salmonella virus P22
Primary publication:
Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity.
Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R
J Mol Biol 293 693-701 (1999)
PMID: 10543960

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-146255 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tail spike protein Chain: A
Molecule details ›
Chain: A
Length: 554 amino acids
Theoretical weight: 59.59 KDa
Source organism: Salmonella virus P22
Expression system: Escherichia coli
UniProt:
  • Canonical: P12528 (Residues: 114-667; Coverage: 83%)
Gene name: 9
Sequence domains: Salmonella phage P22 tail-spike
Structure domains: Pectate Lyase C-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU RU200
Spacegroup: P213
Unit cell:
a: 120.9Å b: 120.9Å c: 120.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The architecture of parallel beta-helices and related folds.
Jenkins et al. (2001)
2 more