2Z7Q: N-terminal kinase domain of human RSK-1

Crystal structure of the N-terminal kinase domain of human RSK-1 bound to AMP-PCP. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 May 2008.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,233
Mol. weight: 37.31 kDa
Ligands: ACP, MG
Released: 13 May 2008

Explore 2Z7Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Z7Q contains 15 α-helices and 9 β-strands across 1 chain. 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: 15 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	59-61	3
β-strand	62-71	10	1
β-strand	74-81	8	1
β-strand	90-95	6	1
β-strand	124	1	2
α-helix	125-126	2
β-strand	127-133	7	1
β-strand	136-141	6	1
β-strand	148	1	2
α-helix	149-156	8
α-helix	161-180	20
α-helix	190-192	3
β-strand	193-195	3	2
β-strand	201-203	3	2
α-helix	226-228	3
α-helix	231-234	4
α-helix	241-257	17
α-helix	267-276	10
α-helix	280-282	3
α-helix	287-296	10
α-helix	312-316	5
α-helix	319-321	3
α-helix	326-330	5
α-helix	335-336	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ribosomal protein S6 kinase alpha-1	A	protein	321	Homo sapiens	Q15418 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2Z7Q_1 Ribosomal protein S6 kinase alpha-1 (chains A)
QPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYA
MKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTR
LSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEA
IDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMFEMLTGSLPFQGKDRKETMT
LILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRR
EIKPPFKPAVAQPDDTFYFDT

Ligands and cofactors

ID	Name	Formula	Copies
ACP	Phosphomethylphosphonic acid adenylate ester	C11 H18 N5 O12 P3	1
MG	Magnesium ion	Mg	1

Primary citation

Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors. Ikuta, M., Kornienko, M., Byrne, N. et al. Protein Sci (2007) 16:2626-2635. DOI 10.1110/ps.073123707 · PubMed

Other PDB entries of the same protein (UniProt Q15418 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5V62 1.9 Å, Phospho-ERK2 bound to bivalent inhibitor SBP3
7P74 1.9 Å, The PDZ domain of SYNJ2BP complexed with the phosphorylated PDZ-binding motif of RSK1
2Z7R 2.0 Å, Crystal Structure of the N-terminal Kinase Domain of Human RSK1 bound to Staurosporine
2Z7S 2.1 Å, Crystal Structure of the N-terminal Kinase Domain of Human RSK1 bound to Purvalnol A
5CSI 2.13 Å, S100B-RSK1 crystal structure A'
4NIF 2.15 Å, Heterodimeric structure of ERK2 and RSK1
5V61 2.2 Å, Phospho-ERK2 bound to bivalent inhibitor SBP2
4H3P 2.3 Å, Crystal structure of human ERK2 complexed with a MAPK docking peptide
5N7D 2.3 Å, MAGI-1 complexed with a RSK1 peptide
5N7F 2.3 Å, MAGI-1 complexed with a pRSK1 peptide
6TWY 2.3 Å, MAGI1_2 complexed with a phosphomimetic RSK1 peptide
2WNT 2.4 Å, Crystal Structure of the Human Ribosomal protein S6 kinase

Browse structure collections

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