Crystal structures of recombinant 19-kda human fibroblast collagenase complexed to itself. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Mar 1995.
Explore 1CGF in 3D Show helices and sheets RCSB PDB PDBe
1CGF contains 7 α-helices and 16 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 113-118 | 6 | 1 |
| α-helix | 127-143 | 17 | |
| β-strand | 148-151 | 4 | 1 |
| β-strand | 159-164 | 6 | 1 |
| β-strand | 182-184 | 3 | 1 |
| β-strand | 195-198 | 4 | 1 |
| β-strand | 204 | 1 | 2 |
| β-strand | 211 | 1 | 2 |
| α-helix | 212-223 | 12 | |
| β-strand | 243 | 1 | 3 |
| β-strand | 245 | 1 | 3 |
| α-helix | 250-257 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 113-118 | 6 | 4 |
| α-helix | 127-142 | 16 | |
| β-strand | 148-151 | 4 | 4 |
| β-strand | 159-164 | 6 | 4 |
| β-strand | 182-184 | 3 | 4 |
| α-helix | 185-186 | 2 | |
| β-strand | 195-198 | 4 | 4 |
| β-strand | 204 | 1 | 5 |
| β-strand | 211 | 1 | 5 |
| α-helix | 212-222 | 11 | |
| α-helix | 250-260 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fibroblast collagenase | A, B | protein | 162 | Homo sapiens | P03956 (AlphaFold model) |
>1CGF_1 FIBROBLAST COLLAGENASE (chains A, B) LTEGNPRWEQTHLRYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMI SFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELG HSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRS
Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Lovejoy, B., Hassell, A.M., Luther, M.A. et al. Biochemistry (1994) 33:8207-8217. DOI 10.1021/bi00193a006 · PubMed
Other PDB entries of the same protein (UniProt P03956 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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