2VWI: OSR1 kinase, a hypertension drug target

Structure of the OSR1 kinase, a hypertension drug target. Determined by X-ray diffraction at 2.15 Å resolution. Released 8 Jul 2008.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 8,508
Mol. weight: 140.25 kDa
Ligands: AU, ANP, MG
Released: 8 Jul 2008

Explore 2VWI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2VWI contains 62 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: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	18-22	5	1
β-strand	31-35	5	1
β-strand	42-46	5	1
β-strand	75	1	2
β-strand	78-83	6	1
β-strand	88-93	6	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	163-164	2
α-helix	166-170	5
α-helix	195-202	8
α-helix	207-222	16
α-helix	232-234	3
α-helix	235-240	6
α-helix	262-271	10
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-286	5

Chain B: 16 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	14-16	3
β-strand	17-24	8	3
β-strand	30-36	7	3
β-strand	41-49	9	3
α-helix	57-69	13
β-strand	75	1	4
β-strand	78-84	7	3
β-strand	87-93	7	3
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
α-helix	155	1
β-strand	160-162	3	4
α-helix	167-173	7
α-helix	195-202	8
α-helix	207-222	16
α-helix	231	1
α-helix	234-241	8
α-helix	246-248	3
α-helix	263-271	9
α-helix	276-278	3
α-helix	280-281	2
α-helix	282-285	4

Chain C: 15 helices, 11 β-strands

Element	Residues	Length	Sheet
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	61-69	9
β-strand	75	1	6
α-helix	76-77	2
β-strand	78-84	7	5
β-strand	87-93	7	5
β-strand	99	1	6
α-helix	100-110	11
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
β-strand	178	1	7
α-helix	190-192	3
α-helix	195-202	8
β-strand	204	1	7
α-helix	207-222	16
α-helix	232-241	10
α-helix	243-245	3
α-helix	263-271	9
α-helix	280-281	2
α-helix	282-285	4

Chain D: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	14-16	3
β-strand	17-25	9	8
β-strand	29-36	8	8
β-strand	41-49	9	8
α-helix	57-67	11
β-strand	75	1	9
β-strand	78-84	7	8
β-strand	87-93	7	8
α-helix	94-95	2
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	190-192	3
α-helix	195-198	4
α-helix	199-201	3
α-helix	207-222	16
α-helix	232-241	10
α-helix	243-245	3
α-helix	255-257	3
α-helix	262-271	10
α-helix	280-281	2
α-helix	282-285	4
α-helix	289-293	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase OSR1	A, B, C, D	protein	303	HOMO SAPIENS	O95747 (AlphaFold model)

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

>2VWI_1 SERINE/THREONINE-PROTEIN KINASE OSR1 (chains A, B, C, D)
MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDEL
LKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDE
STIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRN
KVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTL
QNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFL
QEK

Ligands and cofactors

ID	Name	Formula	Copies
AU	Gold ion	Au	11
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	4
MG	Magnesium ion	Mg	3

Primary citation

Structure of the Osr1 Kinase, a Hypertension Drug Target. Villa, F., Deak, M., Alessi, D.R. et al. Proteins (2008) 73:1082. DOI 10.1002/PROT.22238 · 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
3DAK 2.25 Å, Crystal Structure of Domain-Swapped OSR1 kinase domain

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