3DAK: Domain-Swapped OSR1 kinase domain

Crystal Structure of Domain-Swapped OSR1 kinase domain. Determined by X-ray diffraction at 2.25 Å resolution. Released 10 Feb 2009.

Method: X-ray diffraction
Resolution: 2.25 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,434
Mol. weight: 131.84 kDa
Ligands: ANP, MG
Released: 10 Feb 2009

Explore 3DAK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3DAK contains 73 α-helices and 38 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: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	9-11	3
α-helix	14-16	3
β-strand	17-24	8	1
β-strand	29-36	8	1
α-helix	37-39	3
β-strand	41-49	9	1
α-helix	57-69	13
β-strand	75	1	2
α-helix	76-77	2
β-strand	78-84	7	1
β-strand	87-93	7	1
β-strand	99	1	2
α-helix	100-109	10
α-helix	120-139	20
α-helix	149-151	3
β-strand	152-154	3	2
β-strand	160-162	3	2
α-helix	167-172	6
α-helix	195-202	8
α-helix	207-222	16
α-helix	232-241	10
α-helix	244-245	2
α-helix	254-257	4
α-helix	262-271	10
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-286	5
α-helix	289-293	5

Chain B: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	9-11	3
α-helix	14-16	3
β-strand	17-25	9	3
β-strand	29-36	8	3
β-strand	41-49	9	3
α-helix	57-69	13
β-strand	75	1	4
α-helix	76-77	2
β-strand	78-84	7	3
β-strand	87-93	7	3
α-helix	94-95	2
β-strand	99	1	4
α-helix	100-109	10
α-helix	120-139	20
α-helix	149-151	3
β-strand	152-154	3	4
β-strand	160-162	3	4
α-helix	167-172	6
α-helix	195-202	8
α-helix	207-222	16
α-helix	232-241	10
α-helix	244-245	2
α-helix	254-257	4
α-helix	262-271	10
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-285	4
α-helix	289-293	5

Chain C: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
α-helix	14-16	3
β-strand	17-25	9	5
β-strand	29-36	8	5
β-strand	41-49	9	5
α-helix	57-69	13
β-strand	75	1	6
β-strand	78-84	7	5
β-strand	87-93	7	5
β-strand	99	1	6
α-helix	100-110	11
β-strand	114	1	7
β-strand	116	1	7
α-helix	120-139	20
α-helix	149-151	3
β-strand	152-154	3	6
β-strand	160-162	3	6
α-helix	167-172	6
α-helix	195-201	7
α-helix	207-222	16
α-helix	232-241	10
α-helix	244-246	3
α-helix	262-271	10
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-286	5
α-helix	289-293	5

Chain D: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
α-helix	14-16	3
β-strand	17-24	8	8
β-strand	29-36	8	8
β-strand	41-49	9	8
α-helix	57-67	11
β-strand	75	1	9
α-helix	76-77	2
β-strand	78-84	7	8
β-strand	87-93	7	8
β-strand	99	1	9
α-helix	100-110	11
α-helix	120-139	20
α-helix	149-151	3
β-strand	152-154	3	9
β-strand	160-162	3	9
α-helix	167-172	6
α-helix	175-178	4
α-helix	195-202	8
α-helix	207-222	16
α-helix	232-241	10
α-helix	243-245	3
α-helix	254-257	4
α-helix	262-271	10
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-286	5
α-helix	289-293	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase OSR1	A, B, C, D	protein	290	Homo sapiens	O95747 (AlphaFold model)

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

>3DAK_1 Serine/threonine-protein kinase OSR1 (chains A, B, C, D)
SALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDELLKEIQ
AMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDESTIAT
ILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKT
FVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPP
SLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAK

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	4
MG	Magnesium ion	Mg	4

Primary citation

Crystal structure of domain-swapped STE20 OSR1 kinase domain. Lee, S.J., Cobb, M.H., Goldsmith, E.J. Protein Sci (2008) 18:304-313. DOI 10.1002/pro.27 · PubMed

Other PDB entries of the same protein (UniProt O95747 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7OKW 1.62 Å, 1.62A X-ray crystal structure of the conserved C-terminal (CCT) of human OSR1
2V3S 1.7 Å, Structural insights into the recognition of substrates and activators by the OSR1 kinase
2VWI 2.15 Å, Structure of the OSR1 kinase, a hypertension drug target

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