› 1lla

X-ray diffraction
2.18Å resolution

CRYSTAL STRUCTURE OF DEOXYGENATED LIMULUS POLYPHEMUS SUBUNIT II HEMOCYANIN AT 2.18 ANGSTROMS RESOLUTION: CLUES FOR A MECHANISM FOR ALLOSTERIC REGULATION

Released:
DOI: 10.2210/pdb1lla/pdb
PDB 1lla coloured by chain and viewed from the front.
PDB 1lla coloured by chain and viewed from the side.
PDB 1lla coloured by chain and viewed from the top.
Source organism: Limulus polyphemus
Primary publication:
Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.
Hazes B, Magnus KA, Bonaventura C, Bonaventura J, Dauter Z, Kalk KH, Hol WG
Protein Sci. 2 597-619 (1993)
PMID: 8518732

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemocyanin II Chain: A
Molecule details ›
Chain: A
Length: 628 amino acids
Theoretical weight: 72.76 KDa
Source organism: Limulus polyphemus
Expression system: Not provided
UniProt:
  • Canonical: P04253 (Residues: 1-628; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CU 2 x CU
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 117.002Å b: 117.002Å c: 117.002Å
α: 60.02° β: 60.02° γ: 60.02°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Not provided

Quick links

Citations

10 review citations

Diverse immune functions of hemocyanins.
Coates et al. (2014)
9 more

4 mentions without citation

Copper active sites in biology.
Solomon et al. (2014)
3 more