1BR8: Protein

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.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
3
Atoms
6,526
Mol. weight
99.29 kDa
Released
2 Sept 1998

Explore 1BR8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain I: 15 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand2418
α-helix25-262
α-helix48-6821
β-strand76-7839
α-helix80-9011
α-helix91-933
α-helix96-10510
α-helix108-1114
β-strand11518
α-helix118-13013
β-strand138-1491210
β-strand154111
α-helix156-16611
α-helix1681
β-strand169-173510
α-helix179-19214
β-strand213-2231110
β-strand225112
α-helix228-2303
α-helix231-2333
β-strand235-238413
β-strand248-2571013
β-strand259-26359
β-strand267-27379
β-strand274112
β-strand279-28579
α-helix292-2987
α-helix301-3099
β-strand315-321713
β-strand323-330810
α-helix332-3387
β-strand355111
β-strand364-3751210
β-strand400-403413
β-strand408-41479
β-strand419-42689
Chain L: 14 helices, 24 β-strands
ElementResiduesLengthSheet
α-helix46-6823
β-strand76-7831
α-helix80-9112
α-helix96-10510
α-helix108-1103
α-helix119-13113
β-strand139-14242
β-strand14512
β-strand14613
β-strand14914
β-strand153-15425
α-helix156-1649
β-strand17013
β-strand17314
α-helix175-19319
β-strand214-224112
β-strand22516
β-strand235-23847
α-helix239-2413
β-strand248-25147
β-strand254-26291
α-helix264-2663
β-strand268-27361
β-strand27416
β-strand279-28571
α-helix2861
α-helix293-2975
α-helix301-31010
β-strand312-31871
β-strand32117
β-strand323-33082
α-helix332-3387
α-helix342-3443
β-strand355-35735
β-strand364-375122
β-strand379-390122
β-strand409-41461
β-strand419-42571
Chain P: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2-111010

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (antithrombin-III)I, Lprotein432Homo sapiensP01008 (AlphaFold model)
Protein (peptide)Pprotein12
Sequence of entity 1 (I, L), FASTA
>1BR8_1 PROTEIN (ANTITHROMBIN-III) (chains I, L)
HGSPVDICTAKPRDIPMNPMCIYRSPEKKATEDEGSEQKIPEATNRRVWELSKANSRFAT
TFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQIH
FFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKLQPLDFKENAE
QSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIYFKGLWKSKFSPENTRKELFY
KADGESCSASMMYQEGKFRYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELT
PEVLQEWLDELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRD
DLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTI
IFMGRVANPCVK
Sequence of entity 2 (P), FASTA
>1BR8_2 PROTEIN (PEPTIDE) (chains P)
SEAAASTAVVIA

Primary citation

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:

Browse structure collections

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