5CVA: Collagen alpha-2 chain,Collagen alpha-1 chain
Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest fragment a1a2a1 of type I collagen. Determined by X-ray diffraction at 2.1 Å resolution. Released 10 Aug 2016.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 2,572
- Mol. weight
- 42.2 kDa
- Released
- 10 Aug 2016
Explore 5CVA in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5CVA contains 20 α-helices and 2 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-14 | 5 | |
| α-helix | 16-40 | 25 | |
| α-helix | 41-54 | 14 | |
| α-helix | 56-63 | 8 | |
Chain B: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 16-39 | 24 | |
| α-helix | 42-61 | 20 | |
Chain C: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 13-29 | 17 | |
| α-helix | 31-40 | 10 | |
| α-helix | 41-64 | 24 | |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-23 | 10 | |
| α-helix | 25-40 | 16 | |
| α-helix | 41-54 | 14 | |
| α-helix | 56-63 | 8 | |
Chain E: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16 | 1 | 1 |
| α-helix | 17-40 | 24 | |
| α-helix | 42-58 | 17 | |
Chain F: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-13 | 3 | |
| β-strand | 14 | 1 | 1 |
| α-helix | 15-40 | 26 | |
| α-helix | 41-64 | 24 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain | A, D | protein | 71 | Homo sapiens | P08123 (AlphaFold model), P20849 (AlphaFold model) |
| Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain | B, E | protein | 71 | Homo sapiens | P02452 (AlphaFold model), Q14055 (AlphaFold model) |
| Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain | C, F | protein | 72 | Homo sapiens | P02452 (AlphaFold model), Q14050 |
Sequence of entity 1 (A, D), FASTA
>5CVA_1 Collagen alpha-2(I) chain,Collagen alpha-1(IX) chain (chains A, D)
GSGPPGPPGPPGPPGARGEPGNIGFPGPPGPPGPPGRAPTDQHIKQVCMRVIQEHFAEMA
ASLKRPDSGAT
Sequence of entity 2 (B, E), FASTA
>5CVA_2 Collagen alpha-1(I) chain,Collagen alpha-2(IX) chain (chains B, E)
GSGPPGPPGPPGPPGARGQAGVMGFPGPPGPPGPPGRDATDQHIVDVALKMLQEQLAEVA
VSAKREALGAV
Sequence of entity 3 (C, F), FASTA
>5CVA_3 Collagen alpha-1(I) chain,Collagen alpha-3(IX) chain (chains C, F)
GSGPPGPPGPPGPPGARGQAGVMGFPGPPGPPGPPGKEASEQRIRELCGGMISEQIAQLA
AHLRKPLAPGSI
Primary citation
Structural insight for chain selection and stagger control in collagen. Boudko, S.P., Bachinger, H.P. Sci Rep (2016) 6:37831-37831. DOI 10.1038/srep37831 · PubMed
Other PDB entries of the same protein (UniProt P08123 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5CTD 1.6 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 8YV3 1.68 Å, The heterotrimer structure of peptides derived from human collagen type I
- 5CTI 1.9 Å, Crystal structure of the type IX collagen NC2 hetero-trimerization domain with a guest…
- 6JEC 2.05 Å, Structure of a triple-helix region of human collagen type II
Browse structure collections
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