Hemopexin-like domain of matrix metalloproteinase 14. Determined by X-ray diffraction at 1.7 Å resolution. Released 10 Feb 2009.
Explore 3C7X in 3D Show helices and sheets RCSB PDB PDBe
3C7X contains 10 α-helices and 22 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 318-320 | 3 | |
| β-strand | 325-329 | 5 | 1 |
| β-strand | 332-337 | 6 | 1 |
| β-strand | 340-345 | 6 | 1 |
| β-strand | 348-349 | 2 | 1 |
| α-helix | 350 | 1 | |
| β-strand | 355-356 | 2 | 1 |
| α-helix | 357-360 | 4 | |
| β-strand | 370-373 | 4 | 2 |
| β-strand | 379-383 | 5 | 2 |
| β-strand | 386-391 | 6 | 2 |
| β-strand | 394-395 | 2 | 2 |
| α-helix | 396 | 1 | |
| β-strand | 401-402 | 2 | 2 |
| α-helix | 403-405 | 3 | |
| β-strand | 408 | 1 | 3 |
| β-strand | 417-421 | 5 | 3 |
| β-strand | 426-431 | 6 | 3 |
| β-strand | 434-439 | 6 | 3 |
| β-strand | 444-445 | 2 | 3 |
| α-helix | 446 | 1 | |
| β-strand | 451-452 | 2 | 3 |
| α-helix | 453-455 | 3 | |
| β-strand | 457 | 1 | 4 |
| α-helix | 459-460 | 2 | |
| β-strand | 465-468 | 4 | 4 |
| β-strand | 474-479 | 6 | 4 |
| β-strand | 482-487 | 6 | 4 |
| β-strand | 492-493 | 2 | 4 |
| α-helix | 494 | 1 | |
| β-strand | 499-500 | 2 | 4 |
| α-helix | 501-504 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Matrix metalloproteinase-14 | A | protein | 196 | Homo sapiens | P50281 (AlphaFold model) |
>3C7X_1 Matrix metalloproteinase-14 (chains A) PNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERK DGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKY YRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEP GYPKSALRDWMGCPSG
The dimer interface of the membrane type 1 matrix metalloproteinase hemopexin domain: crystal structure and biological functions. Tochowicz, A., Goettig, P., Evans, R. et al. J Biol Chem (2011) 286:7587-7600. DOI 10.1074/jbc.M110.178434 · PubMed
Other PDB entries of the same protein (UniProt P50281 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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