The 2.6 a structure of antithrombin indicates a conformational change at the heparin binding site. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Jun 1997.
Explore 2ANT in 3D Show helices and sheets RCSB PDB PDBe
2ANT contains 26 α-helices and 40 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-68 | 20 | |
| β-strand | 76-78 | 3 | 6 |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| α-helix | 98-105 | 8 | |
| α-helix | 118-130 | 13 | |
| β-strand | 140-149 | 10 | 7 |
| α-helix | 156-161 | 6 | |
| α-helix | 162-166 | 5 | |
| β-strand | 169-173 | 5 | 7 |
| α-helix | 175-192 | 18 | |
| β-strand | 213-221 | 9 | 7 |
| β-strand | 223-224 | 2 | 7 |
| β-strand | 225 | 1 | 8 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-240 | 6 | 9 |
| β-strand | 246-252 | 7 | 9 |
| β-strand | 255-262 | 8 | 6 |
| β-strand | 268-273 | 6 | 6 |
| β-strand | 274 | 1 | 8 |
| β-strand | 279-285 | 7 | 6 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-319 | 8 | 6 |
| β-strand | 320-321 | 2 | 9 |
| β-strand | 323-330 | 8 | 7 |
| α-helix | 332-338 | 7 | |
| α-helix | 342-344 | 3 | |
| α-helix | 352-354 | 3 | |
| β-strand | 364-375 | 12 | 7 |
| β-strand | 379-380 | 2 | 7 |
| β-strand | 401-403 | 3 | 6 |
| β-strand | 408-414 | 7 | 6 |
| β-strand | 419-426 | 8 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 45-69 | 25 | |
| β-strand | 76-78 | 3 | 1 |
| α-helix | 80-91 | 12 | |
| α-helix | 98-105 | 8 | |
| α-helix | 108-110 | 3 | |
| α-helix | 116-131 | 16 | |
| β-strand | 138-146 | 9 | 2 |
| β-strand | 149 | 1 | 3 |
| β-strand | 154 | 1 | 4 |
| α-helix | 156-165 | 10 | |
| β-strand | 169-170 | 2 | 2 |
| β-strand | 173 | 1 | 3 |
| α-helix | 175-193 | 19 | |
| β-strand | 214-224 | 11 | 2 |
| β-strand | 225 | 1 | 5 |
| β-strand | 235-240 | 6 | 1 |
| β-strand | 246-262 | 17 | 1 |
| α-helix | 264-266 | 3 | |
| β-strand | 268-273 | 6 | 1 |
| β-strand | 274 | 1 | 5 |
| β-strand | 279-285 | 7 | 1 |
| α-helix | 292-297 | 6 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-321 | 10 | 1 |
| β-strand | 323-330 | 8 | 2 |
| α-helix | 332-337 | 6 | |
| α-helix | 342-344 | 3 | |
| β-strand | 355 | 1 | 4 |
| β-strand | 364-375 | 12 | 2 |
| β-strand | 379-390 | 12 | 2 |
| β-strand | 409-414 | 6 | 1 |
| β-strand | 419-425 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antithrombin | I, L | protein | 432 | Homo sapiens | P01008 (AlphaFold model) |
>2ANT_1 ANTITHROMBIN (chains I, L) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAA | 2-acetamido-2-deoxy-beta-D-allopyranose | C8 H15 N O6 | 2 |
The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site. Skinner, R., Abrahams, J.P., Whisstock, J.C. et al. J Mol Biol (1997) 266:601-609. DOI 10.1006/jmbi.1996.0798 · PubMed
Other PDB entries of the same protein (UniProt P01008 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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