Crystal structure of the active form (full-length) of human fibroblast collagenase. Determined by X-ray diffraction at 2.67 Å resolution. Released 9 Aug 2006.
Explore 2CLT in 3D Show helices and sheets RCSB PDB PDBe
2CLT contains 24 α-helices and 54 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 | 83 | 1 | 1 |
| α-helix | 84 | 1 | |
| β-strand | 94-99 | 6 | 2 |
| α-helix | 108-123 | 16 | |
| β-strand | 129-132 | 4 | 2 |
| β-strand | 140-145 | 6 | 2 |
| β-strand | 163-165 | 3 | 2 |
| α-helix | 166-167 | 2 | |
| β-strand | 176-179 | 4 | 2 |
| β-strand | 185 | 1 | 3 |
| β-strand | 192 | 1 | 3 |
| α-helix | 193-205 | 13 | |
| β-strand | 207 | 1 | 1 |
| α-helix | 231-241 | 11 | |
| α-helix | 253-256 | 4 | |
| β-strand | 267-271 | 5 | 4 |
| β-strand | 274-279 | 6 | 4 |
| β-strand | 282-286 | 5 | 4 |
| β-strand | 294-297 | 4 | 4 |
| α-helix | 298-300 | 3 | |
| α-helix | 306 | 1 | |
| β-strand | 311-315 | 5 | 5 |
| β-strand | 320-325 | 6 | 5 |
| β-strand | 328-333 | 6 | 5 |
| β-strand | 336-337 | 2 | 5 |
| α-helix | 338 | 1 | |
| β-strand | 344 | 1 | 5 |
| α-helix | 345-349 | 5 | |
| β-strand | 360-363 | 4 | 6 |
| β-strand | 369-374 | 6 | 6 |
| β-strand | 377-382 | 6 | 6 |
| α-helix | 383-385 | 3 | |
| β-strand | 387-388 | 2 | 6 |
| β-strand | 394-395 | 2 | 6 |
| α-helix | 396-399 | 4 | |
| β-strand | 409-413 | 5 | 7 |
| β-strand | 416-421 | 6 | 7 |
| β-strand | 424-429 | 6 | 7 |
| β-strand | 434-440 | 7 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 83 | 1 | 8 |
| α-helix | 84 | 1 | |
| β-strand | 94-99 | 6 | 9 |
| α-helix | 108-123 | 16 | |
| β-strand | 129-132 | 4 | 9 |
| β-strand | 140-145 | 6 | 9 |
| β-strand | 163-165 | 3 | 9 |
| α-helix | 166-167 | 2 | |
| β-strand | 176-179 | 4 | 9 |
| β-strand | 185 | 1 | 10 |
| β-strand | 192 | 1 | 10 |
| α-helix | 193-204 | 12 | |
| β-strand | 207 | 1 | 8 |
| α-helix | 231-241 | 11 | |
| α-helix | 253-256 | 4 | |
| β-strand | 267-271 | 5 | 11 |
| β-strand | 274-279 | 6 | 11 |
| β-strand | 282-286 | 5 | 11 |
| β-strand | 294-297 | 4 | 11 |
| α-helix | 298-301 | 4 | |
| α-helix | 305-306 | 2 | |
| β-strand | 311-315 | 5 | 12 |
| α-helix | 316-318 | 3 | |
| β-strand | 320-325 | 6 | 12 |
| β-strand | 328-333 | 6 | 12 |
| β-strand | 336-337 | 2 | 12 |
| β-strand | 343-344 | 2 | 12 |
| α-helix | 345-348 | 4 | |
| β-strand | 360-363 | 4 | 13 |
| β-strand | 369-374 | 6 | 13 |
| β-strand | 377-382 | 6 | 13 |
| β-strand | 387-388 | 2 | 13 |
| β-strand | 394-395 | 2 | 13 |
| α-helix | 396-399 | 4 | |
| β-strand | 409-412 | 4 | 14 |
| β-strand | 417-421 | 5 | 14 |
| β-strand | 424-428 | 5 | 14 |
| β-strand | 437-440 | 4 | 14 |
| α-helix | 441-444 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interstitial collagenase | A, B | protein | 367 | HOMO SAPIENS | P03956 (AlphaFold model) |
>2CLT_1 INTERSTITIAL COLLAGENASE (chains A, B) FVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADI MISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHA LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACD SKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDE VRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWR YDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQK ANSWFNC
Crystal Structure of an Active Form of Human Mmp-1. Iyer, S., Visse, R., Nagase, H. et al. J Mol Biol (2006) 362:78. DOI 10.1016/J.JMB.2006.06.079 · 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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