› 1lwu

X-ray diffraction
2.8Å resolution

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

Released:
DOI: 10.2210/pdb1lwu/pdb
PDB entry 1lwu coloured by chain, front view.
PDB entry 1lwu coloured by chain, side view.
PDB entry 1lwu coloured by chain, top view.
Source organism: Petromyzon marinus
Primary publication:
Crystal structure of fragment D from lamprey fibrinogen complexed with the peptide Gly-His-Arg-Pro-amide.
Yang Z, Spraggon G, Pandi L, Everse SJ, Riley M, Doolittle RF
Biochemistry 41 10218-24 (2002)
PMID: 12162736

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-136034 (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%)
Sequence domains: Fibrinogen alpha/beta chain family
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:
Structure domains:
Peptide 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
Carbohydrate polymer
6 bound ligands:
Ligand NDG 9 x NDG
Ligand MAN 10 x MAN
Ligand CA 8 x CA
Ligand NAG 7 x NAG
Ligand BMA 2 x BMA
Ligand GAL 1 x GAL
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

Quick links

Citations

4 review citations

450 million years of hemostasis.
Davidson et al. (2003)
3 more

2 mentions without citation

Rare Variant Analysis of Human and Rodent Obesity Genes in Individuals with Severe Childhood Obesity.
Hendricks et al. (2017)
1 more