1deq

X-ray diffraction
3.5Å resolution

THE CRYSTAL STRUCTURE OF MODIFIED BOVINE FIBRINOGEN (AT ~4 ANGSTROM RESOLUTION)

Released:
Source organism: Bos taurus
Primary publication:
The crystal structure of modified bovine fibrinogen.
Proc. Natl. Acad. Sci. U.S.A. 97 85-90 (2000)
PMID: 10618375

Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only heptamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Fibrinogen alpha chain Chains: A, D, N, Q
Molecule details ›
Chains: A, D, N, Q
Length: 390 amino acids
Theoretical weight: 42.77 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02672 (Residues: 20-409; Coverage: 65%)
Gene name: FGA
Sequence domains: Fibrinogen alpha/beta chain family
Fibrinogen beta chain Chains: B, E, O, R
Molecule details ›
Chains: B, E, O, R
Length: 408 amino acids
Theoretical weight: 46.9 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02676 (Residues: 61-468; Coverage: 87%)
Gene name: FGB
Sequence domains:
Fibrinogen gamma-B chain Chains: C, F, P, S
Molecule details ›
Chains: C, F, P, S
Length: 411 amino acids
Theoretical weight: 46.63 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P12799 (Residues: 25-200, 201-434; Coverage: 97%)
Gene name: FGG
Sequence domains:
FIBRINOGEN Chains: M, Z
Molecule details ›
Chains: M, Z
Length: 90 amino acids
Theoretical weight: 7.68 KDa
Source organism: Bos taurus

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 176.006Å b: 94.935Å c: 209.805Å
α: 90° β: 94.41° γ: 90°
R-values:
R R work R free
0.263 0.257 0.37