5H75: MrsD-Protein A fusion protein

Crystal structure of the MrsD-Protein A fusion protein. Determined by X-ray diffraction at 2.74 Å resolution. Released 28 Jun 2017.

Method
X-ray diffraction
Resolution
2.74 Å
Organisms
Bacillus sp. (strain HIL-Y85/54728), Staphylococcus aureus
Chains
4
Atoms
6,812
Mol. weight
108.21 kDa
Ligands
FAD
Released
28 Jun 2017

Explore 5H75 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5H75 contains 63 α-helices and 33 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.

Chain A: 16 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand10-1561
α-helix19-235
α-helix25-328
β-strand37-4261
α-helix44-496
α-helix52-554
α-helix56-583
β-strand61-6331
α-helix78-814
β-strand84-9071
α-helix92-998
α-helix106-1138
β-strand118-12251
α-helix126-1294
α-helix132-14312
β-strand147-14821
α-helix149-1513
β-strand152-15542
β-strand166-16942
α-helix170-1723
α-helix173-19018
α-helix197-2059
α-helix211-2133
α-helix214-22613
Chain B: 15 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand10-1563
α-helix19-235
α-helix24-329
β-strand37-4263
α-helix44-496
α-helix52-565
β-strand61-6333
α-helix78-814
β-strand84-9073
α-helix92-1009
α-helix106-1138
β-strand118-12253
α-helix126-1294
α-helix132-14312
β-strand147-14823
α-helix149-1513
β-strand15214
β-strand16914
α-helix170-1723
α-helix173-19018
α-helix197-2059
α-helix211-2133
α-helix214-22613
Chain C: 15 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand10-1565
α-helix19-235
α-helix25-328
β-strand37-4265
α-helix44-496
α-helix52-565
β-strand61-6335
α-helix78-814
β-strand84-9075
α-helix92-998
α-helix106-1138
β-strand118-12255
α-helix126-1294
α-helix132-14312
β-strand147-14825
α-helix149-1513
β-strand15216
β-strand16916
α-helix170-1723
α-helix173-19018
α-helix197-2059
α-helix211-2133
α-helix214-22613
Chain D: 17 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix3-64
β-strand10-1567
α-helix19-235
α-helix25-328
β-strand37-4267
α-helix44-496
α-helix52-554
α-helix56-583
β-strand61-6337
α-helix78-814
β-strand84-9077
α-helix92-998
α-helix106-1138
β-strand118-12257
β-strand124-12528
α-helix126-1294
α-helix132-14312
β-strand147-14827
α-helix149-1513
β-strand152-15878
β-strand163-16978
α-helix170-1723
α-helix173-19018
α-helix197-20913
α-helix211-2133
α-helix214-22714

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mersacidin decarboxylase,Immunoglobulin G-binding protein AA, B, C, Dprotein238Bacillus sp. (strain HIL-Y85/54728), Staphylococcus aureusP38507 (AlphaFold model), Q9RC23 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5H75_1 Mersacidin decarboxylase,Immunoglobulin G-binding protein A (chains A, B, C, D)
GSGGGGSMSISILKDKKLLIGICGSISSVGISSYLLYFKSFFKEIRVVMTKTAEDLIPAH
TVSYFCDHVYSEHGENGKRHSHVEIGRWADIYCIIPATANILGQTANGVAMNLVATTVLA
HPHNTIFFPNMNDLMWNKTVVSRNIEQLRKDGHIVIEPVEIMAFEIATGTRKPNRGLITP
DKALLAIEQGFAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK

Ligands and cofactors

IDNameFormulaCopies
FADFlavin-adenine dinucleotideC27 H33 N9 O15 P24

Primary citation

Construction of novel repeat proteins with rigid and predictable structures using a shared helix method. Youn, S.J., Kwon, N.Y., Lee, J.H. et al. Sci Rep (2017) 7:2595-2595. DOI 10.1038/s41598-017-02803-z · PubMed

Other PDB entries of the same protein (UniProt P38507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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