PDBe 5cti

X-ray diffraction
1.9Å resolution

Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a2a1a1 of type I collagen (native form)

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: 7.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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-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 BL21(DE3)
UniProt:
  • Canonical: P02452 (Residues: 572-583; Coverage: 1%)
  • Canonical: Q14050 (Residues: 517-553; Coverage: 6%)
  • nullnull
Gene names: COL1A1, COL9A3
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 BL21(DE3)
UniProt:
  • Canonical: Q14055 (Residues: 517-552; Coverage: 5%)
  • Canonical: P08123 (Residues: 484-495; Coverage: 1%)
  • nullnull
Gene names: COL1A2, COL9A2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-003
Spacegroup: P21
Unit cell:
a: 27.777Å b: 55.912Å c: 61.66Å
α: 90° β: 92.35° γ: 90°
R-values:
R R work R free
0.163 0.16 0.198
Expression system: Escherichia coli BL21(DE3)