4NRH: CopN-Scc3 complex

CopN-Scc3 complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Oct 2014.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Chlamydia pneumoniae
Chains
4
Atoms
7,681
Mol. weight
112.86 kDa
Released
15 Oct 2014

Explore 4NRH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and C: 17 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix96-1027
α-helix109-11810
α-helix125-13511
α-helix139-15214
α-helix155-1573
α-helix158-17518
α-helix177-1837
α-helix186-1938
α-helix200-21112
α-helix217-22711
α-helix230-25021
α-helix257-29337
α-helix304-31512
α-helix322-33312
α-helix337-35014
α-helix356-3583
α-helix362-37918
Chain B: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1311
α-helix25-295
α-helix43-464
α-helix51-6616
α-helix70-8314
α-helix88-10013
α-helix104-11714
α-helix123-13412
α-helix138-15215
α-helix156-1583
α-helix159-16810
Chain D: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1311
α-helix25-295
α-helix43-464
α-helix51-6616
α-helix70-8314
α-helix88-10013
α-helix104-11714
α-helix123-13412
α-helix141-15212
α-helix156-1583
α-helix159-16810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CopNA, Cprotein321Chlamydia pneumoniaeQ9Z8L4 (AlphaFold model)
Chaperone SycDB, Dprotein178Chlamydia pneumoniaeQ9Z6N8 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>4NRH_1 CopN (chains A, C)
GSHMASSESTEEKPDTDLADKYASGNSEISGQELRGLRDAIGDDASPEDILALVQEKIKD
PALQSTALDYLVQTTPPSQGKLKEALIQARNTHTEQFGRTAIGAKNILFASQEYADQLNV
SPSGLRSLYLEVTGDTHTCDQLLSMLQDRYTYQDMAIVSSFLMKGMATGLKRQGPYVPSA
QLQVLMTETRNLQAVLTSYDYFESRVPILLDSLKAEGIQTPSDLNFVKVAESYHKIINDK
FPTASKVEREVRNLIGDDVDSVTGVLNLFFSALRQTSSRLFSSADKRQQLGAMIANALDA
VNINNEDYPKASDFPKPYPWS
Sequence of entity 2 (B, D), FASTA
>4NRH_2 Chaperone SycD (chains B, D)
GSHMASMSHLNYLLEKIAASSKEDFPFPDDLESYLEGYVPDKNIALDTYQKIFKISSEDL
EKVYKEGYHAYLDKDYAKSITVFRWLVFFNPFVSKFWFSLGASLHMSEQYSQALHAYGVT
AVLRDKDPYPHYYAYICYTLTNEHEEAEKALEMAWVRAQHKPLYNELKEEILDIRKHK

Primary citation

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:

Browse structure collections

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