Crystal structure of the MrsD-Protein A fusion protein. Determined by X-ray diffraction at 2.74 Å resolution. Released 28 Jun 2017.
Explore 5H75 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 1 |
| α-helix | 19-23 | 5 | |
| α-helix | 25-32 | 8 | |
| β-strand | 37-42 | 6 | 1 |
| α-helix | 44-49 | 6 | |
| α-helix | 52-55 | 4 | |
| α-helix | 56-58 | 3 | |
| β-strand | 61-63 | 3 | 1 |
| α-helix | 78-81 | 4 | |
| β-strand | 84-90 | 7 | 1 |
| α-helix | 92-99 | 8 | |
| α-helix | 106-113 | 8 | |
| β-strand | 118-122 | 5 | 1 |
| α-helix | 126-129 | 4 | |
| α-helix | 132-143 | 12 | |
| β-strand | 147-148 | 2 | 1 |
| α-helix | 149-151 | 3 | |
| β-strand | 152-155 | 4 | 2 |
| β-strand | 166-169 | 4 | 2 |
| α-helix | 170-172 | 3 | |
| α-helix | 173-190 | 18 | |
| α-helix | 197-205 | 9 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 3 |
| α-helix | 19-23 | 5 | |
| α-helix | 24-32 | 9 | |
| β-strand | 37-42 | 6 | 3 |
| α-helix | 44-49 | 6 | |
| α-helix | 52-56 | 5 | |
| β-strand | 61-63 | 3 | 3 |
| α-helix | 78-81 | 4 | |
| β-strand | 84-90 | 7 | 3 |
| α-helix | 92-100 | 9 | |
| α-helix | 106-113 | 8 | |
| β-strand | 118-122 | 5 | 3 |
| α-helix | 126-129 | 4 | |
| α-helix | 132-143 | 12 | |
| β-strand | 147-148 | 2 | 3 |
| α-helix | 149-151 | 3 | |
| β-strand | 152 | 1 | 4 |
| β-strand | 169 | 1 | 4 |
| α-helix | 170-172 | 3 | |
| α-helix | 173-190 | 18 | |
| α-helix | 197-205 | 9 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 5 |
| α-helix | 19-23 | 5 | |
| α-helix | 25-32 | 8 | |
| β-strand | 37-42 | 6 | 5 |
| α-helix | 44-49 | 6 | |
| α-helix | 52-56 | 5 | |
| β-strand | 61-63 | 3 | 5 |
| α-helix | 78-81 | 4 | |
| β-strand | 84-90 | 7 | 5 |
| α-helix | 92-99 | 8 | |
| α-helix | 106-113 | 8 | |
| β-strand | 118-122 | 5 | 5 |
| α-helix | 126-129 | 4 | |
| α-helix | 132-143 | 12 | |
| β-strand | 147-148 | 2 | 5 |
| α-helix | 149-151 | 3 | |
| β-strand | 152 | 1 | 6 |
| β-strand | 169 | 1 | 6 |
| α-helix | 170-172 | 3 | |
| α-helix | 173-190 | 18 | |
| α-helix | 197-205 | 9 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-226 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| β-strand | 10-15 | 6 | 7 |
| α-helix | 19-23 | 5 | |
| α-helix | 25-32 | 8 | |
| β-strand | 37-42 | 6 | 7 |
| α-helix | 44-49 | 6 | |
| α-helix | 52-55 | 4 | |
| α-helix | 56-58 | 3 | |
| β-strand | 61-63 | 3 | 7 |
| α-helix | 78-81 | 4 | |
| β-strand | 84-90 | 7 | 7 |
| α-helix | 92-99 | 8 | |
| α-helix | 106-113 | 8 | |
| β-strand | 118-122 | 5 | 7 |
| β-strand | 124-125 | 2 | 8 |
| α-helix | 126-129 | 4 | |
| α-helix | 132-143 | 12 | |
| β-strand | 147-148 | 2 | 7 |
| α-helix | 149-151 | 3 | |
| β-strand | 152-158 | 7 | 8 |
| β-strand | 163-169 | 7 | 8 |
| α-helix | 170-172 | 3 | |
| α-helix | 173-190 | 18 | |
| α-helix | 197-209 | 13 | |
| α-helix | 211-213 | 3 | |
| α-helix | 214-227 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mersacidin decarboxylase,Immunoglobulin G-binding protein A | A, B, C, D | protein | 238 | Bacillus sp. (strain HIL-Y85/54728), Staphylococcus aureus | P38507 (AlphaFold model), Q9RC23 (AlphaFold model) |
>5H75_1 Mersacidin decarboxylase,Immunoglobulin G-binding protein A (chains A, B, C, D) GSGGGGSMSISILKDKKLLIGICGSISSVGISSYLLYFKSFFKEIRVVMTKTAEDLIPAH TVSYFCDHVYSEHGENGKRHSHVEIGRWADIYCIIPATANILGQTANGVAMNLVATTVLA HPHNTIFFPNMNDLMWNKTVVSRNIEQLRKDGHIVIEPVEIMAFEIATGTRKPNRGLITP DKALLAIEQGFAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| FAD | Flavin-adenine dinucleotide | C27 H33 N9 O15 P2 | 4 |
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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