9IVT: Ang1 receptor-binding domain

Crystal structure of Ang1 receptor-binding domain. Determined by X-ray diffraction at 1.75 Å resolution. Released 2 Jul 2025.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
1
Atoms
1,900
Mol. weight
26.19 kDa
Released
2 Jul 2025

Explore 9IVT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9IVT contains 8 α-helices and 19 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.

Chain A: 8 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix286-2916
β-strand298-30251
β-strand30512
β-strand30712
β-strand311-31661
α-helix319-3213
β-strand324-33071
α-helix341-3466
β-strand348-34921
β-strand355-35621
α-helix359-3668
β-strand371-37881
β-strand384-394111
α-helix397-3993
β-strand403-41081
β-strand421-42331
β-strand42613
β-strand42714
β-strand43014
α-helix439-4435
β-strand44713
β-strand455-45625
α-helix464-4663
β-strand475-47625
α-helix477-4804
β-strand48115
β-strand488-49581

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Angiopoietin-1Aprotein229Homo sapiensQ15389 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9IVT_1 Angiopoietin-1 (chains A)
DYKDDDDKGGGGSFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQH
REDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQY
DRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWF
DACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF

Primary citation

Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice. Wang, R., Li, H., Xie, Z. et al. Sci Adv (2025) 11:eads1796-eads1796. DOI 10.1126/sciadv.ads1796 · PubMed

Other PDB entries of the same protein (UniProt Q15389 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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