High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria meningitidis in fusion with MBP. Determined by X-ray diffraction at 1.43 Å resolution. Released 18 May 2016.
Explore 5HZ7 in 3D Show helices and sheets RCSB PDB PDBe
5HZ7 contains 28 α-helices and 36 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 | 2-4 | 3 | |
| β-strand | 7 | 1 | 1 |
| β-strand | 10-11 | 2 | 2 |
| α-helix | 18-32 | 15 | |
| β-strand | 35 | 1 | 1 |
| β-strand | 39 | 1 | 2 |
| α-helix | 44-52 | 9 | |
| β-strand | 60-64 | 5 | 2 |
| α-helix | 65-67 | 3 | |
| α-helix | 68-73 | 6 | |
| β-strand | 77 | 1 | 3 |
| α-helix | 78-79 | 2 | |
| β-strand | 80 | 1 | 4 |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 5 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 107-112 | 6 | 2 |
| β-strand | 115-119 | 5 | 6 |
| β-strand | 129 | 1 | 7 |
| α-helix | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 6 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 8 |
| β-strand | 176-183 | 8 | 8 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 6 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-238 | 6 | |
| β-strand | 243-246 | 4 | 6 |
| α-helix | 247-249 | 3 | |
| β-strand | 250 | 1 | 7 |
| β-strand | 251 | 1 | 9 |
| β-strand | 254 | 1 | 9 |
| α-helix | 258 | 1 | |
| β-strand | 259-260 | 2 | 10 |
| β-strand | 261-267 | 7 | 2 |
| β-strand | 268 | 1 | 3 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 2 |
| β-strand | 305 | 1 | 5 |
| α-helix | 306-312 | 7 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 10 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-370 | 13 | |
| α-helix | 372-373 | 2 | |
| α-helix | 374-401 | 28 | |
| β-strand | 407 | 1 | 11 |
| β-strand | 410 | 1 | 11 |
| α-helix | 411-414 | 4 | |
| β-strand | 418-419 | 2 | 12 |
| β-strand | 422-427 | 6 | 12 |
| β-strand | 439-444 | 6 | 12 |
| β-strand | 453-457 | 5 | 12 |
| β-strand | 462-467 | 6 | 12 |
| β-strand | 478-479 | 2 | 12 |
| β-strand | 484-488 | 5 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ComP | A | protein | 490 | Neisseria meningitidis | P0AEX9 (AlphaFold model) |
>5HZ7_1 ComP (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYAAGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAAAASEFEKAKINAVRAALLENAHFMEKFYLQNGRFKQTSTKWPSLPIKEAE GFCIRLNGIARGALDSKFMLKAVAIDKDKNPFIIKMNENLVTFICKKSASSCSDGLDYFK GNDKDCKLFK
| ID | Name | Formula | Copies |
|---|---|---|---|
| BGC | beta-D-glucopyranose | C6 H12 O6 | 1 |
Water and common crystallization additives (NA, EDO) are not listed.
A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding. Berry, J.L., Xu, Y., Ward, P.N. et al. Structure (2016) 24:926-934. DOI 10.1016/j.str.2016.04.001 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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