› 2hlo

X-ray diffraction
2.6Å resolution

Crystal Structure of Fragment D-dimer from Human Fibrin Complexed with Gly-hydroxyPro-Arg-Pro-amide

Released:
DOI: 10.2210/pdb2hlo/pdb
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PDB entry 2hlo coloured by chain, front view.
PDB entry 2hlo coloured by chain, side view.
PDB entry 2hlo coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Doolittle RF, Kollman JM, Chen A, Pandi L

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-136007 (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
UniProt:
  • Canonical: P02671 (Residues: 130-216; Coverage: 10%)
Gene name: FGA
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
Molecule details ›
Chains: B, E
Length: 328 amino acids
Theoretical weight: 37.69 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02675 (Residues: 164-491; Coverage: 71%)
Gene name: FGB
Sequence domains:
Structure domains:
Fibrinogen gamma chain Chains: C, F
GLY-HYP-ARG-PRO-AMIDE PEPTIDE LIGAND Chains: G, H

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
1 bound ligand:
Ligand CA 7 x CA
1 modified residue:
Ligand HYP 2 x HYP

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P212121
Unit cell:
a: 54.69Å b: 149.48Å c: 232.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.21 0.268

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