4K0V: Angiopoietin-1 mediated signaling initiation

Structural basis for angiopoietin-1 mediated signaling initiation. Determined by X-ray diffraction at 4.51 Å resolution. Released 8 May 2013.

Method: X-ray diffraction
Resolution: 4.51 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,775
Mol. weight: 85.21 kDa
Released: 8 May 2013

Explore 4K0V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4K0V contains 18 α-helices and 79 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: 13 helices, 63 β-strands

Element	Residues	Length	Sheet
β-strand	25-31	7	1
β-strand	34-35	2	2
β-strand	40-47	8	1
α-helix	54-55	2
β-strand	56-59	4	3
β-strand	64	1	4
α-helix	67-69	3
β-strand	75-77	3	1
β-strand	82-88	7	1
α-helix	89	1
β-strand	98-103	6	3
β-strand	112-117	6	3
β-strand	118-119	2	2
β-strand	124-125	2	5
β-strand	130-134	5	6
β-strand	139-140	2	7
β-strand	144-145	2	5
β-strand	153-157	5	6
β-strand	158	1	4
β-strand	160-165	6	6
β-strand	173	1	5
β-strand	177-178	2	7
β-strand	187-192	6	6
β-strand	204-209	6	6
β-strand	215-216	2	8
β-strand	222-223	2	8
α-helix	224-226	3
β-strand	232-233	2	9
β-strand	240-241	2	9
β-strand	246-247	2	10
β-strand	253-254	2	10
α-helix	255-256	2
β-strand	259-260	2	11
β-strand	266-267	2	11
β-strand	278-281	4	1
β-strand	286-289	4	1
β-strand	291	1	12
β-strand	294	1	13
β-strand	300	1	13
α-helix	301-303	3
β-strand	306	1	14
β-strand	309	1	12
β-strand	314	1	14
β-strand	323-324	2	15
β-strand	328-329	2	15
α-helix	331-332	2
β-strand	335	1	16
β-strand	343	1	16
α-helix	347-350	4
β-strand	352	1	17
β-strand	358	1	18
β-strand	362	1	19
β-strand	366	1	20
β-strand	369-372	4	17
α-helix	380-382	3
β-strand	383-386	4	18
β-strand	392-393	2	18
β-strand	397-399	3	17
β-strand	405-408	4	17
β-strand	411	1	20
α-helix	416-418	3
β-strand	420-428	9	18
β-strand	431-439	9	18
α-helix	441	1
β-strand	442	1	19
α-helix	443-444	2
β-strand	447	1	21
α-helix	450-451	2
β-strand	452-455	4	22
β-strand	462-464	3	22
β-strand	470	1	21
β-strand	480-484	5	23
β-strand	494	1	23
β-strand	499-501	3	22
β-strand	511-516	6	23
β-strand	533-534	2	23

Chain B: 5 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	7-12	6
β-strand	19-23	5	24
β-strand	32-37	6	24
β-strand	45-50	6	24
α-helix	62-67	6
β-strand	69-70	2	24
β-strand	76-77	2	24
α-helix	80-86	7
β-strand	92-99	8	24
β-strand	105-115	11	24
β-strand	124-131	8	24
β-strand	146-148	3	25
β-strand	151	1	25
α-helix	161-164	4
β-strand	167-169	3	25
β-strand	176-177	2	26
β-strand	181	1	27
β-strand	194	1	27
β-strand	196-197	2	26
α-helix	198-201	4
β-strand	211-216	6	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
TEK tyrosine kinase variant	A	protein	529	Homo sapiens	Q02763 (AlphaFold model)
Angiopoietin-1	B	protein	230	Homo sapiens	Q15389 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4K0V_1 TEK tyrosine kinase variant (chains A)
AMDLILINSLPLVSDAETSLTCIASGWRPHEPITIGRDFEALMNQHQDPLEVTQDVTREW
AKKVVWKREKASKINGAYFCEGRVRGEAIRIRTMKMRQQASFLPATLTMTVDKGDNVNIS
FKKVLIKEEDAVIYKNGSFIHSVPRHEVPDILEVHLPHAQPQDAGVYSARYIGGNLFTSA
FTRLIVRRCEAQKWGPECNHLCTACMNNGVCHEDTGECICPPGFMGRTCEKACELHTFGR
TCKERCSGQEGCKSYVFCLPDPYGCSCATGWKGLQCNEACHPGFYGPDCKLRCSCNNGEM
CDRFQGCLCSPGWQGLQCEREGIPRMTPKIVDLPDHIEVNSGKFNPICKASGWPLPTNEE
MTLVKPDGTVLHPKDFNHTDHFSVAIFTIHRILPPDSGVWVCSVNTVAGMVEKPFNISVK
VLPKPLNAPNVIDTGHNFAVINISSEPYFGDGPIKSKKLLYKPVNHYEAWQHIQVTNEIV
TLNYLEPRTEYELCVQLVRRGEGGEGHPGPVRRFTTASIGGSASGLVPR

Sequence of entity 2 (B), FASTA

>4K0V_2 Angiopoietin-1 (chains B)
AELASEKPFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQHREDGS
LDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHI
GNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGP
SNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDFGSLVPR

Primary citation

Structural basis for angiopoietin-1-mediated signaling initiation. Yu, X., Seegar, T.C., Dalton, A.C. et al. Proc Natl Acad Sci U S A (2013) 110:7205-7210. DOI 10.1073/pnas.1216890110 · PubMed

Other PDB entries of the same protein (UniProt Q02763 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BEA 2.02 Å, cFMS tyrosine kinase (tie2 KID) in complex with a pyrimidinopyridone inhibitor
6MWE 2.05 Å, Crystal structure of TIE2 in complex with decipera compound DP1919
7E72 2.09 Å, Crystal structure of Tie2-agonistic antibody in complex with human Tie2 Fn2-3
1FVR 2.2 Å, TIE2 kinase domain
2OO8 2.2 Å, Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent,…
3L8P 2.4 Å, Crystal structure of cytoplasmic kinase domain of Tie2 complexed with inhibitor CEP11207
2P4I 2.5 Å, Evolution of a highly Selective and Potent 2-(Pyridin-2-yl)-1,3,5-triazine Tie-2 Kinase…
4X3J 2.5 Å, Selection of fragments for kinase inhibitor design: decoration is key
5UTK 2.5 Å, Crystal structure of the membrane proximal three fibronectin type III (FNIII) domains of…
5MYB 2.6 Å, Homodimerization of Tie2 Fibronectin-like domains 2 and 3 in space group P21
9LV4 2.67 Å, Cryo-EM Structure of Human Tie2/minibinder tw1102_4 helices Complex
2OSC 2.8 Å, Synthesis, Structural Analysis, and SAR Studies of Triazine Derivatives as Potent,…

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