› 2h43

X-ray diffraction
2.7Å resolution

Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide

Released:
DOI: 10.2210/pdb2h43/pdb
PDB entry 2h43 coloured by chain, front view.
PDB entry 2h43 coloured by chain, side view.
PDB entry 2h43 coloured by chain, top view.
Source organisms:
Primary publication:
Differences in binding specificity for the homologous gamma- and beta-chain "holes" on fibrinogen: exclusive binding of Ala-His-Arg-Pro-amide by the beta-chain hole.
Doolittle RF, Chen A, Pandi L
Biochemistry 45 13962-9 (2006)
PMID: 17115691

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-136006 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (6 distinct):
Fibrinogen alpha chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 87 amino acids
Theoretical weight: 10.24 KDa
Source organism: Homo sapiens
Fibrinogen beta chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 328 amino acids
Theoretical weight: 37.69 KDa
Source organism: Homo sapiens
Fibrinogen gamma chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 323 amino acids
Theoretical weight: 36.56 KDa
Source organism: Homo sapiens
GLY-HIS-ARG-PRO-AMIDE peptide ligand Chains: I, J
Molecule details ›
Chains: I, J
Length: 5 amino acids
Theoretical weight: 480 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
1 bound ligand:
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 105Å b: 47.9Å c: 171.4Å
α: 90° β: 105.41° γ: 90°
R-values:
R R work R free
0.244 0.251 0.307
Expression system: Not provided

Quick links

Citations

2 review citations

A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers.
Guthold et al. (2007)
1 more

2 mentions without citation

Lessons from the Crystal Structure of the S. aureus Surface Protein Clumping Factor A in Complex With Tefibazumab, an Inhibiting Monoclonal Antibody.
Ganesh et al. (2016)
1 more