3OP5: Human vaccinia-related kinase 1

Human vaccinia-related kinase 1. Determined by X-ray diffraction at 2.4 Å resolution. Released 22 Sept 2010.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,797
Mol. weight: 166.37 kDa
Ligands: REB
Released: 22 Sept 2010

Explore 3OP5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3OP5 contains 70 α-helices and 48 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: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	28-30	3	1
β-strand	36-42	7	1
β-strand	50-56	7	1
α-helix	61-62	2
β-strand	68-74	7	1
α-helix	78-90	13
α-helix	93-102	10
α-helix	111-112	2
β-strand	113-121	9	1
β-strand	124-132	9	1
β-strand	134-137	4	2
α-helix	138-144	7
α-helix	151-170	20
β-strand	173-174	2	3
α-helix	180-182	3
β-strand	183-186	4	2
β-strand	193-195	3	2
β-strand	202-203	2	3
α-helix	206-208	3
α-helix	210-212	3
α-helix	230-233	4
α-helix	236-238	3
α-helix	240-256	17
α-helix	262-264	3
α-helix	268-280	13
α-helix	282-289	8
α-helix	297-307	11
α-helix	313-315	3
α-helix	317-330	14

Chain B: 17 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	28-30	3	4
β-strand	36-42	7	4
β-strand	50-56	7	4
α-helix	61-62	2
β-strand	68-74	7	4
α-helix	78-90	13
α-helix	93-102	10
α-helix	111-112	2
β-strand	113-121	9	4
β-strand	124-132	9	4
β-strand	134-137	4	5
α-helix	138-144	7
α-helix	151-170	20
β-strand	173-174	2	6
α-helix	180-182	3
β-strand	183-186	4	5
β-strand	193-195	3	5
β-strand	202-203	2	6
α-helix	206-208	3
α-helix	210-212	3
α-helix	230-233	4
α-helix	240-256	17
α-helix	262-264	3
α-helix	268-280	13
α-helix	282-289	8
α-helix	297-307	11
α-helix	313-315	3
α-helix	317-330	14

Chain C: 17 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	28-30	3	7
β-strand	36-45	10	7
β-strand	50-56	7	7
β-strand	68-72	5	7
α-helix	81-90	10
α-helix	93-102	10
α-helix	111-112	2
β-strand	113-120	8	7
β-strand	125-132	8	7
β-strand	134-137	4	8
α-helix	138-144	7
α-helix	151-170	20
β-strand	173-174	2	9
α-helix	180-182	3
β-strand	183-186	4	8
β-strand	193-195	3	8
β-strand	202-203	2	9
α-helix	206-208	3
α-helix	210-213	4
β-strand	215	1	10
α-helix	230-233	4
β-strand	236	1	10
α-helix	237-238	2
α-helix	240-256	17
α-helix	262-264	3
α-helix	268-280	13
α-helix	282-289	8
α-helix	297-307	11
α-helix	313-315	3
α-helix	317-330	14

Chain D: 18 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	28-30	3	11
β-strand	36-42	7	11
β-strand	51-56	6	11
β-strand	68-74	7	11
α-helix	80-90	11
α-helix	93-103	11
α-helix	111-112	2
β-strand	113-119	7	11
β-strand	126-132	7	11
β-strand	134-137	4	12
α-helix	138-144	7
α-helix	151-170	20
β-strand	173-174	2	13
α-helix	180-182	3
β-strand	183-186	4	12
β-strand	193-195	3	12
β-strand	202-203	2	13
α-helix	206-208	3
α-helix	210-213	4
β-strand	215	1	14
α-helix	217-219	3
α-helix	230-233	4
β-strand	236	1	14
α-helix	237-238	2
α-helix	240-256	17
α-helix	262-264	3
α-helix	268-280	13
α-helix	282-289	8
α-helix	297-307	11
α-helix	313-315	3
α-helix	317-330	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase VRK1	A, B, C, D	protein	364	Homo sapiens	Q99986 (AlphaFold model)

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

>3OP5_1 Serine/threonine-protein kinase VRK1 (chains A, B, C, D)
SMRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAAAAWKVGLPIGQGGFGCIYLADMNSSE
SVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHD
KNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKA
SNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKAYAADPKRCHDGTIEFTSIDAHNGVAPSR
RGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPAANAPGEIA
KYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKKRAA
EIEE

Ligands and cofactors

ID	Name	Formula	Copies
REB	[4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]pyrimidin-2-yl}amino)phenyl]aceton…	C18 H17 N7	4

Water and common crystallization additives (EDO, GOL) are not listed.

Primary citation

Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations. Counago, R.M., Allerston, C.K., Savitsky, P. et al. Sci Rep (2017) 7:7501-7501. DOI 10.1038/s41598-017-07755-y · PubMed

Other PDB entries of the same protein (UniProt Q99986 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7M10 1.15 Å, PHF2 PHD Domain Complexed with Peptide From N-terminus of VRK1
6BRU 1.8 Å, Crystal Structure of the Human vaccinia-related kinase bound to a…
6BU6 1.8 Å, Crystal Structure of the Human vaccinia-related kinase bound to a…
6BP0 1.9 Å, Crystal Structure of the Human vaccinia-related kinase 1 bound to…
6BTW 1.9 Å, Crystal Structure of the Human vaccinia-related kinase bound to a phenyl-pteridinone…
5UVF 2.0 Å, Crystal Structure of the Human vaccinia-related kinase bound to BI-D1870
6CNX 2.0 Å, Crystal Structure of the Human vaccinia-related kinase 1 (VRK1) bound to an…
6VXU 2.0 Å, Structure of Human Vaccinia-related Kinase 1 (VRK1) bound to ACH471
9ZKG 2.06 Å, VRK1 in complex with the inhibitor MP-60
6AC9 2.07 Å, Crystal structure of human Vaccinia-related kinase 1 (VRK1) in complex with AMP-PNP
6CMM 2.1 Å, Crystal Structure of the Human vaccinia-related kinase bound to a…
6DD4 2.1 Å, Crystal Structure of the Human vaccinia-related kinase bound to a…

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