Crystal structure of Annexin A2 complexed with S100A4. Determined by X-ray diffraction at 2.1 Å resolution. Released 5 Jul 2017.
Explore 5LPU in 3D Show helices and sheets RCSB PDB PDBe
5LPU contains 54 α-helices and 4 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 | 4-12 | 9 | |
| α-helix | 20-22 | 3 | |
| α-helix | 35-47 | 13 | |
| α-helix | 53-60 | 8 | |
| α-helix | 65-79 | 15 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-103 | 11 | |
| α-helix | 106-118 | 13 | |
| α-helix | 125-134 | 10 | |
| α-helix | 137-151 | 15 | |
| α-helix | 155-162 | 8 | |
| α-helix | 165-175 | 11 | |
| α-helix | 179-183 | 5 | |
| α-helix | 188-201 | 14 | |
| α-helix | 210-219 | 10 | |
| α-helix | 222-235 | 14 | |
| α-helix | 240-247 | 8 | |
| α-helix | 250-279 | 30 | |
| α-helix | 285-294 | 10 | |
| α-helix | 300-311 | 12 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-335 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| α-helix | 24-30 | 7 | |
| α-helix | 33-47 | 15 | |
| α-helix | 53-60 | 8 | |
| α-helix | 65-79 | 15 | |
| α-helix | 83-90 | 8 | |
| α-helix | 93-103 | 11 | |
| α-helix | 106-118 | 13 | |
| α-helix | 125-134 | 10 | |
| α-helix | 137-150 | 14 | |
| α-helix | 155-159 | 5 | |
| α-helix | 165-175 | 11 | |
| α-helix | 179-182 | 4 | |
| α-helix | 188-201 | 14 | |
| α-helix | 210-219 | 10 | |
| α-helix | 222-235 | 14 | |
| α-helix | 240-247 | 8 | |
| α-helix | 250-279 | 30 | |
| α-helix | 285-295 | 11 | |
| α-helix | 300-311 | 12 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-335 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-20 | 17 | |
| β-strand | 29 | 1 | 1 |
| α-helix | 31-41 | 11 | |
| α-helix | 43-46 | 4 | |
| α-helix | 52-62 | 11 | |
| β-strand | 70 | 1 | 1 |
| α-helix | 72-88 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-20 | 17 | |
| β-strand | 29 | 1 | 2 |
| α-helix | 31-41 | 11 | |
| α-helix | 43-45 | 3 | |
| α-helix | 52-62 | 11 | |
| β-strand | 70 | 1 | 2 |
| α-helix | 72-91 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Annexin A2 | A, B | protein | 339 | Homo sapiens | P07355 (AlphaFold model) |
| Protein S100-A4 | C, D | protein | 104 | Homo sapiens | P26447 (AlphaFold model) |
>5LPU_1 Annexin A2 (chains A, B) XSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNIL TNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKG LGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRA EDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDM LESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDM LKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
>5LPU_2 Protein S100-A4 (chains C, D) GSHMACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQK LMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 14 |
Water and common crystallization additives (GOL) are not listed.
Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. Ecsedi, P., Kiss, B., Gogl, G. et al. Structure (2017) 25:1195-1207.e5. DOI 10.1016/j.str.2017.06.001 · PubMed
Other PDB entries of the same protein (UniProt P07355 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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