5CBN: Maltose-binding periplasmic protein

Fusion protein of mbp3-16 and B4 domain of protein A from staphylococcal aureus with chemical cross-linker EY-CBS. Determined by X-ray diffraction at 2.3 Å resolution. Released 30 Mar 2016.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Escherichia coli (strain K12), synthetic construct, Staphylococcus aureus
Chains
2
Atoms
4,295
Mol. weight
60.21 kDa
Ligands
EYC
Released
30 Mar 2016

Explore 5CBN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CBN contains 35 α-helices and 26 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.

Chain A: 10 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix14-2411
α-helix27-359
α-helix50-578
α-helix60-689
α-helix83-897
α-helix93-1019
α-helix116-1227
α-helix126-122922
α-helix1235-124612
α-helix1252-126514
Chain B: 25 helices, 26 β-strands
ElementResiduesLengthSheet
β-strand7-1041
α-helix17-3115
β-strand35-3841
α-helix43-519
β-strand59-6351
α-helix64-663
α-helix67-726
β-strand7612
α-helix77-793
α-helix83-864
β-strand8913
α-helix91-955
β-strand98-9924
β-strand102-10324
β-strand106-11161
β-strand114-11855
β-strand12816
α-helix129-1313
α-helix132-14110
β-strand145-14735
α-helix154-1618
β-strand16717
β-strand17018
α-helix172-1743
β-strand17718
β-strand18217
α-helix186-20015
α-helix210-2189
β-strand222-22765
α-helix229-2313
α-helix232-2387
β-strand242-24545
α-helix246-2483
β-strand24916
β-strand25019
β-strand25319
α-helix254-2552
β-strand258-259210
β-strand260-26671
β-strand26712
α-helix273-2797
α-helix280-2845
α-helix287-29610
β-strand301-30221
β-strand30413
α-helix305-3117
α-helix315-32612
β-strand328-329210
α-helix330-3312
α-helix336-35217
α-helix357-3637

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic proteinBprotein369Escherichia coli (strain K12)P0AEX9 (AlphaFold model)
mbp3-16,Immunoglobulin G-binding protein AAprotein176synthetic construct, Staphylococcus aureusP38507 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>5CBN_1 Maltose-binding periplasmic protein (chains B)
MGMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP
DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY
NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD
IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT
SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK
PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV
DEALKDAQT
Sequence of entity 2 (A), FASTA
>5CBN_2 mbp3-16,Immunoglobulin G-binding protein A (chains A)
SDLGKKLLEAAHAGQDDEVRILMANGADVNAMDNFGVTPLHLAAYWGHFEIVEVLLKYGA
DVNASDATGDTPLHLAAKWGYLGIVEVLLKYGADVNAQDKFGKTAFDISIDNGNEDLAEI
LCKNKAQQAAFYCILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK

Ligands and cofactors

IDNameFormulaCopies
EYC2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid}C18 H14 Cl2 N2 O8 S21

Primary citation

Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Jeong, W.H., Lee, H., Song, D.H. et al. Nat Commun (2016) 7:11031-11031. DOI 10.1038/ncomms11031 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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