Implications for function and therapy of a 2.9A structure of binary-complexed antithrombin. Determined by X-ray diffraction at 2.9 Å resolution. Released 2 Sept 1998.
Explore 1BR8 in 3D Show helices and sheets RCSB PDB PDBe
1BR8 contains 29 α-helices and 46 β-strands across 3 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 | 24 | 1 | 8 |
| α-helix | 25-26 | 2 | |
| α-helix | 48-68 | 21 | |
| β-strand | 76-78 | 3 | 9 |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-111 | 4 | |
| β-strand | 115 | 1 | 8 |
| α-helix | 118-130 | 13 | |
| β-strand | 138-149 | 12 | 10 |
| β-strand | 154 | 1 | 11 |
| α-helix | 156-166 | 11 | |
| α-helix | 168 | 1 | |
| β-strand | 169-173 | 5 | 10 |
| α-helix | 179-192 | 14 | |
| β-strand | 213-223 | 11 | 10 |
| β-strand | 225 | 1 | 12 |
| α-helix | 228-230 | 3 | |
| α-helix | 231-233 | 3 | |
| β-strand | 235-238 | 4 | 13 |
| β-strand | 248-257 | 10 | 13 |
| β-strand | 259-263 | 5 | 9 |
| β-strand | 267-273 | 7 | 9 |
| β-strand | 274 | 1 | 12 |
| β-strand | 279-285 | 7 | 9 |
| α-helix | 292-298 | 7 | |
| α-helix | 301-309 | 9 | |
| β-strand | 315-321 | 7 | 13 |
| β-strand | 323-330 | 8 | 10 |
| α-helix | 332-338 | 7 | |
| β-strand | 355 | 1 | 11 |
| β-strand | 364-375 | 12 | 10 |
| β-strand | 400-403 | 4 | 13 |
| β-strand | 408-414 | 7 | 9 |
| β-strand | 419-426 | 8 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 46-68 | 23 | |
| β-strand | 76-78 | 3 | 1 |
| α-helix | 80-91 | 12 | |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| α-helix | 119-131 | 13 | |
| β-strand | 139-142 | 4 | 2 |
| β-strand | 145 | 1 | 2 |
| β-strand | 146 | 1 | 3 |
| β-strand | 149 | 1 | 4 |
| β-strand | 153-154 | 2 | 5 |
| α-helix | 156-164 | 9 | |
| β-strand | 170 | 1 | 3 |
| β-strand | 173 | 1 | 4 |
| α-helix | 175-193 | 19 | |
| β-strand | 214-224 | 11 | 2 |
| β-strand | 225 | 1 | 6 |
| β-strand | 235-238 | 4 | 7 |
| α-helix | 239-241 | 3 | |
| β-strand | 248-251 | 4 | 7 |
| β-strand | 254-262 | 9 | 1 |
| α-helix | 264-266 | 3 | |
| β-strand | 268-273 | 6 | 1 |
| β-strand | 274 | 1 | 6 |
| β-strand | 279-285 | 7 | 1 |
| α-helix | 286 | 1 | |
| α-helix | 293-297 | 5 | |
| α-helix | 301-310 | 10 | |
| β-strand | 312-318 | 7 | 1 |
| β-strand | 321 | 1 | 7 |
| β-strand | 323-330 | 8 | 2 |
| α-helix | 332-338 | 7 | |
| α-helix | 342-344 | 3 | |
| β-strand | 355-357 | 3 | 5 |
| β-strand | 364-375 | 12 | 2 |
| β-strand | 379-390 | 12 | 2 |
| β-strand | 409-414 | 6 | 1 |
| β-strand | 419-425 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-11 | 10 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (antithrombin-III) | I, L | protein | 432 | Homo sapiens | P01008 (AlphaFold model) |
| Protein (peptide) | P | protein | 12 |
>1BR8_1 PROTEIN (ANTITHROMBIN-III) (chains I, L) HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH FFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD DLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI IFMGRVANPCVK
>1BR8_2 PROTEIN (PEPTIDE) (chains P) SEAAASTAVVIA
Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin. Skinner, R., Chang, W.S., Jin, L. et al. J Mol Biol (1998) 283:9-14. DOI 10.1006/jmbi.1998.2083 · 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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