PDBe 5ctd

X-ray diffraction
1.6Å resolution

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 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
Sequence domain:

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 Chain: A
Molecule details ›
Chain: A
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-2(I) chain; Collagen alpha-2(IX) chain Chain: B
Molecule details ›
Chain: B
Length: 71 amino acids
Theoretical weight: 6.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14055 (Residues: 517-552; Coverage: 5%)
  • Canonical: P08123 (Residues: 484-495; Coverage: 1%)
  • nullnull
Gene names: COL1A2, COL9A2
Collagen alpha-1(I) chain; Collagen alpha-3(IX) chain Chain: C
Molecule details ›
Chain: C
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

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 27.89Å b: 55.92Å c: 62.1Å
α: 90° β: 92.86° γ: 90°
R-values:
R R work R free
0.179 0.177 0.202
Expression system: Escherichia coli