Structure analysis

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

X-ray diffraction
1.599Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 12474.67 Å2
Buried surface area: 9556.77 Å2
Dissociation area: 3,127.27 Å2
Dissociation energy (ΔGdiss): 45.61 kcal/mol
Dissociation entropy (TΔSdiss): 12.6 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-135848

Macromolecules

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

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Chain: B
Length: 71 amino acids
Theoretical weight: 6.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14055 (Residues: 496-496, 517-552; Coverage: 6%)
  • Canonical: P08123 (Residues: 485-495; Coverage: 1%)
  • nullnull
Gene names: COL1A2, COL9A2
Pfam: Collagen triple helix repeat (20 copies)
InterPro: Collagen triple helix repeat

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Chain: C
Length: 72 amino acids
Theoretical weight: 7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02452 (Residues: 573-583; Coverage: 1%)
  • Canonical: Q14050 (Residues: 496-496, 517-553; Coverage: 6%)
  • nullnull
Gene names: COL1A1, COL9A3
Pfam: Collagen triple helix repeat (20 copies)

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