PDBe 5cvb

X-ray diffraction
2.25Å resolution

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a1a1 of type I collagen

Released:
Source organism: Homo sapiens

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Collagen alpha-1(I) chain; Collagen alpha-1(IX) chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 71 amino acids
Theoretical weight: 7.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02452 (Residues: 572-583; Coverage: 1%)
  • Canonical: P20849 (Residues: 754-789; Coverage: 4%)
  • nullnull
Gene names: COL1A1, COL9A1
Collagen alpha-1(I) chain; Collagen alpha-2(IX) chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 71 amino acids
Theoretical weight: 6.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14055 (Residues: 496-496, 517-552; Coverage: 6%)
  • Canonical: P02452 (Residues: 573-583; Coverage: 1%)
  • nullnull
Gene names: COL1A1, COL9A2
Collagen alpha-1(I) chain; Collagen alpha-3(IX) chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 72 amino acids
Theoretical weight: 7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02452 (Residues: 572-583; Coverage: 1%)
  • Canonical: Q14050 (Residues: 517-553; Coverage: 6%)
  • nullnull
Gene names: COL1A1, COL9A3

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 51.77Å b: 64.46Å c: 65.39Å
α: 90° β: 112.72° γ: 90°
R-values:
R R work R free
0.232 0.227 0.278
Expression system: Escherichia coli