4EPU: Ang1 fibrinogen-related domain

Ang1 fibrinogen-related domain (FReD). Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Apr 2013.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,752
Mol. weight: 50.65 kDa
Ligands: CA
Released: 17 Apr 2013

Explore 4EPU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4EPU contains 15 α-helices and 38 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, 19 β-strands

Element	Residues	Length	Sheet
α-helix	286-291	6
β-strand	298-302	5	1
β-strand	311-316	6	1
α-helix	319-321	3
β-strand	324-330	7	1
α-helix	341-346	6
β-strand	348-349	2	1
β-strand	355-356	2	1
α-helix	359-366	8
β-strand	371-378	8	1
β-strand	384-394	11	1
α-helix	397-399	3
β-strand	403-410	8	1
β-strand	423	1	1
β-strand	426	1	2
β-strand	427	1	3
β-strand	430	1	3
α-helix	439-443	5
β-strand	447	1	2
β-strand	455-456	2	4
β-strand	460	1	5
β-strand	473	1	5
β-strand	475-476	2	4
β-strand	481	1	4
α-helix	484-486	3
β-strand	488-495	8	1

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	286-291	6
β-strand	298-302	5	6
β-strand	311-316	6	6
α-helix	319-321	3
β-strand	324-330	7	6
α-helix	341-346	6
β-strand	348-349	2	6
β-strand	355-356	2	6
α-helix	359-366	8
β-strand	371-378	8	6
β-strand	384-394	11	6
α-helix	397-399	3
β-strand	403-410	8	6
β-strand	423	1	6
β-strand	426	1	7
β-strand	427	1	8
β-strand	430	1	8
α-helix	439-443	5
β-strand	447	1	7
β-strand	455-456	2	9
β-strand	460	1	10
β-strand	473	1	10
β-strand	475-476	2	9
α-helix	477-480	4
β-strand	481	1	9
α-helix	484-486	3
β-strand	488-495	8	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Angiopoietin-1	A, B	protein	221	Homo sapiens	Q15389 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4EPU_1 Angiopoietin-1 (chains A, B)
ADPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQR
GWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQ
NYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNG
MFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDGGR

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2

Primary citation

Biochemical and structural characterization of the Ang1 fibrinogen-related domain. Yeykal, C.C., Sundaresan, L., Mrksich, M. et al. To be published.

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

9IVT 1.75 Å, Crystal structure of Ang1 receptor-binding domain
9IVU 2.28 Å, Crystal structure of Ang1-A451D receptor binding domain
4JYO 2.5 Å, Structural basis for angiopoietin-1 mediated signaling initiation
4K0V 4.51 Å, Structural basis for angiopoietin-1 mediated signaling initiation

Browse structure collections

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