1Z3U: Angiopoietin-2

Structure of the Angiopoietin-2 Recptor Binding Domain and Identification of Surfaces Involved in Tie2 Recognition. Determined by X-ray diffraction at 2.25 Å resolution. Released 12 Jul 2005.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Homo sapiens
Chains: 4
Atoms: 7,259
Mol. weight: 98.55 kDa
Ligands: CA
Released: 12 Jul 2005

Explore 1Z3U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Z3U contains 28 α-helices and 64 β-strands across 4 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, 16 β-strands

Element	Residues	Length	Sheet
β-strand	281	1	1
α-helix	284-288	5
β-strand	296-301	6	1
β-strand	308-314	7	1
β-strand	322-328	7	1
α-helix	339-344	6
β-strand	346-347	2	1
β-strand	353-354	2	1
α-helix	357-366	10
β-strand	369-376	8	1
β-strand	382-392	11	1
α-helix	395-397	3
β-strand	401-408	8	1
α-helix	421-423	3
β-strand	424	1	2
β-strand	425	1	3
β-strand	428	1	3
α-helix	437-441	5
β-strand	445	1	2
β-strand	453-454	2	4
β-strand	473-474	2	4
α-helix	475-478	4
β-strand	486-493	8	1

Chain B: 7 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	281	1	5
α-helix	284-288	5
β-strand	296-301	6	5
β-strand	308-314	7	5
β-strand	322-328	7	5
α-helix	339-344	6
β-strand	346-347	2	5
β-strand	353-354	2	5
α-helix	357-366	10
β-strand	369-376	8	5
β-strand	382-392	11	5
α-helix	395-397	3
β-strand	401-408	8	5
α-helix	421-423	3
β-strand	424	1	6
β-strand	425	1	7
β-strand	428	1	7
α-helix	437-441	5
β-strand	445	1	6
β-strand	453-454	2	8
β-strand	458	1	9
β-strand	471	1	9
β-strand	473-474	2	8
α-helix	475-478	4
β-strand	486-493	8	5

Chains C and D: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	284-289	6
β-strand	296-301	6	10
β-strand	308-314	7	10
β-strand	322-328	7	10
α-helix	339-344	6
β-strand	346-347	2	10
β-strand	353-354	2	10
α-helix	357-364	8
β-strand	369-376	8	10
β-strand	382-392	11	10
α-helix	395-397	3
β-strand	401-408	8	10
α-helix	421-423	3
β-strand	424	1	11
β-strand	425	1	12
β-strand	428	1	12
α-helix	437-441	5
β-strand	445	1	11
β-strand	453-454	2	13
β-strand	473-474	2	13
α-helix	475-478	4
β-strand	486-493	8	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-2	A, B, C, D	protein	217	Homo sapiens	O15123 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1Z3U_1 Angiopoietin-2 (chains A, B, C, D)
SFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTW
KEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNY
RIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMY
YPQRQNTNKANGIKWAAWKGSGYSLKATTMMIRPADF

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

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:

4JZC 1.9 Å, Angiopoietin-2 fibrinogen domain TAG mutant
4ZFG 2.27 Å, Dual-specificity Fab 5A12 in complex with Angiopoietin 2
1Z3S 2.35 Å, Angiopoietin-2 Receptor Binding Domain
8VGP 2.7 Å, CryoEM structure of Angiopoietin-2 in complex with engineered conformationally rigid Fab…
9HMI 2.87 Å, Crystal structure of the Calf domains of Integrin Alpha5 in complex with angiopoietin2…
2GY7 3.7 Å, Angiopoietin-2/Tie2 Complex Crystal Structure

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