CopN-Scc3 complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Oct 2014.
Explore 4NRH in 3D Show helices and sheets RCSB PDB PDBe
4NRH contains 56 α-helices and 0 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 | 96-102 | 7 | |
| α-helix | 109-118 | 10 | |
| α-helix | 125-135 | 11 | |
| α-helix | 139-152 | 14 | |
| α-helix | 155-157 | 3 | |
| α-helix | 158-175 | 18 | |
| α-helix | 177-183 | 7 | |
| α-helix | 186-193 | 8 | |
| α-helix | 200-211 | 12 | |
| α-helix | 217-227 | 11 | |
| α-helix | 230-250 | 21 | |
| α-helix | 257-293 | 37 | |
| α-helix | 304-315 | 12 | |
| α-helix | 322-333 | 12 | |
| α-helix | 337-350 | 14 | |
| α-helix | 356-358 | 3 | |
| α-helix | 362-379 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 25-29 | 5 | |
| α-helix | 43-46 | 4 | |
| α-helix | 51-66 | 16 | |
| α-helix | 70-83 | 14 | |
| α-helix | 88-100 | 13 | |
| α-helix | 104-117 | 14 | |
| α-helix | 123-134 | 12 | |
| α-helix | 138-152 | 15 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-168 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-13 | 11 | |
| α-helix | 25-29 | 5 | |
| α-helix | 43-46 | 4 | |
| α-helix | 51-66 | 16 | |
| α-helix | 70-83 | 14 | |
| α-helix | 88-100 | 13 | |
| α-helix | 104-117 | 14 | |
| α-helix | 123-134 | 12 | |
| α-helix | 141-152 | 12 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-168 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CopN | A, C | protein | 321 | Chlamydia pneumoniae | Q9Z8L4 (AlphaFold model) |
| Chaperone SycD | B, D | protein | 178 | Chlamydia pneumoniae | Q9Z6N8 (AlphaFold model) |
>4NRH_1 CopN (chains A, C) GSHMASSESTEEKPDTDLADKYASGNSEISGQELRGLRDAIGDDASPEDILALVQEKIKD PALQSTALDYLVQTTPPSQGKLKEALIQARNTHTEQFGRTAIGAKNILFASQEYADQLNV SPSGLRSLYLEVTGDTHTCDQLLSMLQDRYTYQDMAIVSSFLMKGMATGLKRQGPYVPSA QLQVLMTETRNLQAVLTSYDYFESRVPILLDSLKAEGIQTPSDLNFVKVAESYHKIINDK FPTASKVEREVRNLIGDDVDSVTGVLNLFFSALRQTSSRLFSSADKRQQLGAMIANALDA VNINNEDYPKASDFPKPYPWS
>4NRH_2 Chaperone SycD (chains B, D) GSHMASMSHLNYLLEKIAASSKEDFPFPDDLESYLEGYVPDKNIALDTYQKIFKISSEDL EKVYKEGYHAYLDKDYAKSITVFRWLVFFNPFVSKFWFSLGASLHMSEQYSQALHAYGVT AVLRDKDPYPHYYAYICYTLTNEHEEAEKALEMAWVRAQHKPLYNELKEEILDIRKHK
A gatekeeper chaperone complex directs translocator secretion during type three secretion. Archuleta, T.L., Spiller, B.W. PLoS Pathog (2014) 10:e1004498-e1004498. DOI 10.1371/journal.ppat.1004498 · PubMed
Other PDB entries of the same protein (UniProt Q9Z8L4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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