Human Annexin A2 with heparin hexasaccharide bound. Determined by X-ray diffraction at 1.42 Å resolution. Released 5 Sept 2006.
Explore 2HYV in 3D Show helices and sheets RCSB PDB PDBe
2HYV contains 21 α-helices and 0 β-strands across 1 chain. 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 | 34-46 | 13 | |
| α-helix | 52-59 | 8 | |
| α-helix | 64-78 | 15 | |
| α-helix | 82-89 | 8 | |
| α-helix | 92-102 | 11 | |
| α-helix | 105-116 | 12 | |
| α-helix | 124-133 | 10 | |
| α-helix | 136-150 | 15 | |
| α-helix | 154-160 | 7 | |
| α-helix | 164-174 | 11 | |
| α-helix | 178-182 | 5 | |
| α-helix | 187-199 | 13 | |
| α-helix | 209-218 | 10 | |
| α-helix | 221-231 | 11 | |
| α-helix | 239-246 | 8 | |
| α-helix | 249-263 | 15 | |
| α-helix | 265-277 | 13 | |
| α-helix | 284-294 | 11 | |
| α-helix | 299-310 | 12 | |
| α-helix | 314-321 | 8 | |
| α-helix | 324-334 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Annexin A2 | A | protein | 308 | Homo sapiens | P07355 (AlphaFold model) |
>2HYV_1 Annexin A2 (chains A) NFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSAL SGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMY KTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVP KWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFA DRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKAL LYLCGGDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 5 |
Crystallographic analysis of calcium-dependent heparin binding to annexin A2. Shao, C., Zhang, F., Kemp, M.M. et al. J Biol Chem (2006) 281:31689-31695. DOI 10.1074/jbc.M604502200 · 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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