7PQS: SRPK1

SRPK1 in complex with MSC2711186. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Dec 2021.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,947
Mol. weight: 88.75 kDa
Ligands: 80H, CIT
Released: 15 Dec 2021

Explore 7PQS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7PQS contains 48 α-helices and 30 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: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	75-76	2	1
β-strand	80-88	9	1
β-strand	92-99	8	1
β-strand	104-111	8	1
α-helix	115-133	19
α-helix	139-143	5
β-strand	144	1	2
β-strand	147-155	9	1
β-strand	158-165	8	1
β-strand	170-171	2	2
α-helix	172-178	7
α-helix	186-202	17
α-helix	203-207	5
β-strand	209-210	2	3
α-helix	216-218	3
β-strand	219-221	3	2
α-helix	222	1
α-helix	225-237	13
α-helix	268-273	6
β-strand	276-278	3	2
α-helix	281-283	3
β-strand	285-286	2	3
β-strand	289	1	3
α-helix	298-300	3
α-helix	303-307	5
α-helix	314-329	16
α-helix	344-356	13
α-helix	359-360	2
α-helix	361-366	6
α-helix	370-373	4
β-strand	374	1	4
β-strand	380	1	4
α-helix	391-397	7
α-helix	403-413	11
α-helix	414-417	4
α-helix	421-423	3
α-helix	425-426	2
α-helix	427-430	4
α-helix	434-437	4

Chain B: 24 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	75-76	2	5
β-strand	80-88	9	5
β-strand	92-99	8	5
β-strand	104-111	8	5
α-helix	115-133	19
α-helix	139-143	5
β-strand	144	1	6
β-strand	149-155	7	5
β-strand	158-165	8	5
β-strand	170-171	2	6
α-helix	172-178	7
α-helix	186-202	17
α-helix	203-207	5
β-strand	209-210	2	7
α-helix	216-218	3
β-strand	219-221	3	6
α-helix	222	1
α-helix	225-236	12
α-helix	268-273	6
β-strand	276-278	3	6
α-helix	281-283	3
β-strand	285-286	2	7
β-strand	289	1	7
α-helix	298-300	3
α-helix	303-307	5
α-helix	314-329	16
α-helix	344-356	13
α-helix	359-360	2
α-helix	361-366	6
α-helix	370-373	4
β-strand	374	1	8
β-strand	380	1	8
α-helix	391-397	7
α-helix	403-413	11
α-helix	414-417	4
α-helix	421-423	3
α-helix	425-426	2
α-helix	427-430	4
α-helix	434-437	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SRSF protein kinase 1	A, B	protein	383	Homo sapiens	Q96SB4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7PQS_1 SRSF protein kinase 1 (chains A, B)
SMDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAE
HYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKW
IIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEA
TEWQRSGAPPPSGSAVSTAPATAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDI
QTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIEL
LGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLP
MLELIPEKRATAAECLRHPWLNS

Ligands and cofactors

ID	Name	Formula	Copies
80H	~{N}-[3-[[[2-(6-chloranyl-7-fluoranyl-1~{H}-benzimidazol-2-yl)pyrimidin-4-yl]am…	C19 H17 Cl F N7 O2 S	2
CIT	Citric acid	C6 H8 O7	1

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

Primary citation

SRPK1 in complex with MSC2711186. Schroeder, M., Leiendecker, M., Knapp, S. To be published.

Other PDB entries of the same protein (UniProt Q96SB4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NNG 1.2 Å, Crystal Structure of the first bromodomain of human BRD4 in complex with an acetylated…
5MY8 1.7 Å, Crystal structure of SRPK1 in complex with SPHINX31
1WAK 1.73 Å, X-ray structure of SRPK1
5MXX 1.75 Å, Crystal structure of human SR protein kinase 1 (SRPK1) in complex with compound 1
4WUA 2.0 Å, Crystal structure of human SRPK1 complexed to an inhibitor SRPIN340
7DD1 2.05 Å, Crystal structure of SRPK1 in complex with a peptide inhibitor
7ZKS 2.28 Å, SRPK1 in complex with inhibitor
5XV7 2.32 Å, SRPK1 in complex with Alectinib
1WBP 2.4 Å, SRPK1 bound to 9mer docking motif peptide
6FAD 2.8 Å, SR protein kinase 1 (SRPK1) in complex with the RGG-box of HSV1 ICP27
3BEG 2.9 Å, Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2

Browse structure collections

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