› 1ypa

X-ray diffraction
2Å resolution

DIRECT OBSERVATION OF BETTER HYDRATION AT THE N-TERMINUS OF AN ALPHA-HELIX WITH GLYCINE RATHER THAN ALANINE AS N-CAP

Released:
DOI: 10.2210/pdb1ypa/pdb
PDB entry 1ypa coloured by chain, front view.
PDB entry 1ypa coloured by chain, side view.
PDB entry 1ypa coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue.
Harpaz Y, Elmasry N, Fersht AR, Henrick K
Proc Natl Acad Sci U S A 91 311-5 (1994)
PMID: 8278384

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133913 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Subtilisin-chymotrypsin inhibitor-2A Chain: I
Molecule details ›
Chain: I
Length: 64 amino acids
Theoretical weight: 7.18 KDa
Source organism: Hordeum vulgare
Expression system: Not provided
UniProt:
  • Canonical: P01053 (Residues: 21-84; Coverage: 76%)
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 29.13Å b: 33.62Å c: 56.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Is there a unifying mechanism for protein folding?
Daggett et al. (2003)
1 more

8 mentions without citation

An all-atom structure-based potential for proteins: bridging minimal models with all-atom empirical forcefields.
Whitford et al. (2009)
7 more