Research workbench
Crystal structure of human fibrillar procollagen type III C- propeptide trimer
Analyse Crystal structure of human fibrillar procollagen type III C- propeptide trimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AEJ
- Type
- protein
- Length
- 643 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02461
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 213 | — | P02461 |
| B | — | protein | 218 | — | P02461 |
| C | — | protein | 212 | — | P02461 |
Compared structures
- 4AEJ · Crystal structure of Human fibrillar procollagen type III C- propeptide trimer · the same entry in another collection · chain A against A, TM-score 1.00
- P02461 · AlphaFold monomer V2.0 prediction for collagen alpha-1(III) chain (P02461) · a predicted model of the same protein · chain C against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P02461
- Elsewhere: RCSB PDB 4AEJ · PDBe 4AEJ · UniProt P02461
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