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X-ray diffraction
2.8Å resolution

Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (5 distinct):
Fibrinogen alpha-1 chain Chains: A, D, G, J
Molecule details ›
Chains: A, D, G, J
Length: 119 amino acids
Theoretical weight: 14.07 KDa
Source organism: Petromyzon marinus
UniProt:
  • Canonical: P02674 (Residues: 87-205; Coverage: 12%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Fibrinogen beta chain Chains: B, E, H, K
Molecule details ›
Chains: B, E, H, K
Length: 323 amino acids
Theoretical weight: 37.06 KDa
Source organism: Petromyzon marinus
UniProt:
  • Canonical: P02678 (Residues: 155-477; Coverage: 68%)
Structure domains:
Fibrinogen gamma chain Chains: C, F, I, L
Molecule details ›
Chains: C, F, I, L
Length: 323 amino acids
Theoretical weight: 37.48 KDa
Source organism: Petromyzon marinus
UniProt:
  • Canonical: P04115 (Residues: 103-425; Coverage: 79%)
Gene name: FGG
Sequence domains: Fibrinogen beta and gamma chains, C-terminal globular domain
Structure domains:
Ligand Gly-His-Arg-Pro-NH2 Chains: M, N, O, P
Molecule details ›
Chains: M, N, O, P
Length: 5 amino acids
Theoretical weight: 466 Da

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P1
Unit cell:
a: 76.735Å b: 47.654Å c: 244.65Å
α: 88.81° β: 97.23° γ: 86.17°
R-values:
R R work R free
0.251 0.245 0.287