human Zn MATCAP. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 May 2022.
Explore 7Z5H in 3D Show helices and sheets RCSB PDB PDBe
7Z5H contains 108 α-helices and 28 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 148-157 | 10 | |
| β-strand | 165 | 1 | 1 |
| α-helix | 172 | 1 | |
| α-helix | 174-179 | 6 | |
| α-helix | 188-202 | 15 | |
| α-helix | 205-213 | 9 | |
| β-strand | 216 | 1 | 2 |
| α-helix | 217-218 | 2 | |
| α-helix | 219-233 | 15 | |
| β-strand | 240-244 | 5 | 3 |
| β-strand | 251-256 | 6 | 3 |
| β-strand | 259-265 | 7 | 3 |
| β-strand | 270 | 1 | 2 |
| α-helix | 271-280 | 10 | |
| α-helix | 281-286 | 6 | |
| α-helix | 287-293 | 7 | |
| α-helix | 300-306 | 7 | |
| α-helix | 308-310 | 3 | |
| α-helix | 314-323 | 10 | |
| α-helix | 333-345 | 13 | |
| α-helix | 350-356 | 7 | |
| α-helix | 357-359 | 3 | |
| α-helix | 364-374 | 11 | |
| β-strand | 380 | 1 | 1 |
| α-helix | 388-391 | 4 | |
| α-helix | 392-402 | 11 | |
| α-helix | 409-414 | 6 | |
| α-helix | 420-422 | 3 | |
| α-helix | 423-426 | 4 | |
| α-helix | 427-429 | 3 | |
| α-helix | 435-438 | 4 | |
| α-helix | 439-441 | 3 | |
| α-helix | 444-457 | 14 | |
| α-helix | 462-468 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 148-157 | 10 | |
| β-strand | 165 | 1 | 4 |
| α-helix | 172 | 1 | |
| α-helix | 174-179 | 6 | |
| α-helix | 188-202 | 15 | |
| α-helix | 205-213 | 9 | |
| β-strand | 216 | 1 | 5 |
| α-helix | 217-218 | 2 | |
| α-helix | 219-233 | 15 | |
| β-strand | 240-244 | 5 | 6 |
| β-strand | 251-256 | 6 | 6 |
| β-strand | 259-265 | 7 | 6 |
| β-strand | 270 | 1 | 5 |
| α-helix | 271-280 | 10 | |
| α-helix | 281-286 | 6 | |
| α-helix | 287-293 | 7 | |
| α-helix | 300-305 | 6 | |
| α-helix | 308-310 | 3 | |
| α-helix | 314-323 | 10 | |
| α-helix | 333-345 | 13 | |
| α-helix | 350-356 | 7 | |
| α-helix | 357-359 | 3 | |
| α-helix | 364-374 | 11 | |
| β-strand | 380 | 1 | 4 |
| α-helix | 388-391 | 4 | |
| α-helix | 392-402 | 11 | |
| α-helix | 409-414 | 6 | |
| α-helix | 420-422 | 3 | |
| α-helix | 423-426 | 4 | |
| α-helix | 427-429 | 3 | |
| α-helix | 435-438 | 4 | |
| α-helix | 439-441 | 3 | |
| α-helix | 444-457 | 14 | |
| α-helix | 462-468 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uncharacterized protein KIAA0895-like | A, B, C, D | protein | 335 | Homo sapiens | Q68EN5 (AlphaFold model) |
>7Z5H_1 Uncharacterized protein KIAA0895-like (chains A, B, C, D) PCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKYCEASGQFIHQAVGIIE AVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVVVQLSEDLLSQAVMMVE NSRPTLAINLTGARQYWLEGMLRHEIGTHYLRGVNNARQPWHNAEGRLRYGLRPANPTEE GLASLHSVLFRKQPFLWRAALLYYTIHRAARMSFRQLFQDLERYVQDADVRWEYCVRAKR GQTDTSLPGCFSKDQVYLDGIVRILRHRQTIDFPLLTSLGKVSYEDVDHLRPHGVLDNTR VPHFMQDLARYRQQLEHIMATNRLDEAELGRLLPD
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Posttranslational modification of microtubules by the MATCAP detyrosinase. Landskron, L., Bak, J., Adamopoulos, A. et al. Science (2022) 376:eabn6020-eabn6020. DOI 10.1126/science.abn6020 · PubMed
Other PDB entries of the same protein (UniProt Q68EN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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