1Z3S: Angiopoietin-2 Receptor Binding Domain

Angiopoietin-2 Receptor Binding Domain. Determined by X-ray diffraction at 2.35 Å resolution. Released 12 Jul 2005.

Method
X-ray diffraction
Resolution
2.35 Å
Organism
Homo sapiens
Chains
2
Atoms
3,697
Mol. weight
49.88 kDa
Ligands
CA
Released
12 Jul 2005

Explore 1Z3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z3S contains 13 α-helices and 30 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.

Chain A: 7 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix284-2885
β-strand296-30161
β-strand308-31471
β-strand322-32871
α-helix339-3446
β-strand34711
β-strand35311
α-helix357-36610
β-strand369-37681
β-strand382-392111
α-helix395-3973
β-strand401-40881
α-helix421-4233
β-strand42412
β-strand42513
β-strand42813
α-helix437-4415
β-strand44512
β-strand453-45424
β-strand473-47424
α-helix475-4784
β-strand486-49381
Chain B: 6 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix284-2885
β-strand296-30165
β-strand308-31475
β-strand322-32875
α-helix339-3446
β-strand34716
β-strand35316
α-helix357-36610
β-strand369-37685
β-strand382-392115
α-helix395-3973
β-strand401-40885
β-strand42417
β-strand42518
β-strand42818
α-helix437-4415
β-strand44517
β-strand453-45429
β-strand473-47429
α-helix475-4784
β-strand486-49275

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Angiopoietin-2A, Bprotein217Homo sapiensO15123 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1Z3S_1 Angiopoietin-2 (chains A, B)
EFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTW
KEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNY
RIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMY
YPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

Primary citation

Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition. Barton, W.A., Tzvetkova, D., Nikolov, D.B. Structure (2005) 13:825-832. DOI 10.1016/j.str.2005.03.009 · PubMed

Other PDB entries of the same protein (UniProt O15123 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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