› 1rc9

X-ray diffraction
1.6Å resolution

Crystal Structure of Stecrisp, a Member of CRISP Family from Trimeresurus Stejnegeri Refined at 1.6 Angstroms Resolution: Structual relationship of the two domains

Released:
DOI: 10.2210/pdb1rc9/pdb
PDB entry 1rc9 coloured by chain, front view.
PDB entry 1rc9 coloured by chain, side view.
PDB entry 1rc9 coloured by chain, top view.
Source organism: Trimeresurus stejnegeri
Primary publication:
Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel inhibitor-like fold.
Guo M, Teng M, Niu L, Liu Q, Huang Q, Hao Q
J Biol Chem 280 12405-12 (2005)
PMID: 15596436

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cysteine-rich venom protein Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 25.15 KDa
Source organism: Trimeresurus stejnegeri
UniProt:
  • Canonical: P60623 (Residues: 13-233; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: I222
Unit cell:
a: 61.381Å b: 78.421Å c: 106.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.219

Quick links

Citations

15 review citations

Fertilization Mechanisms in Flowering Plants.
Dresselhaus et al. (2016)
14 more

6 mentions without citation

Cysteine-Rich Secretory Proteins (CRISPs) From Venomous Snakes: An Overview of the Functional Diversity in A Large and Underappreciated Superfamily.
Tadokoro et al. (2020)
5 more