2ERZ: C-AMP Dependent Kinase

Crystal Structure of c-AMP Dependent Kinase (PKA) bound to hydroxyfasudil. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 Nov 2005.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,016
Mol. weight: 43.32 kDa
Ligands: HFS
Released: 8 Nov 2005

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

Secondary structure: helices and β-sheets

2ERZ contains 20 α-helices and 15 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 E: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	16-31	16
α-helix	40-42	3
β-strand	43-51	9	1
β-strand	56-62	7	1
β-strand	67-75	9	1
α-helix	76-81	6
α-helix	85-95	11
β-strand	103	1	2
β-strand	106-111	6	1
β-strand	115-121	7	1
β-strand	127	1	2
α-helix	128-135	8
α-helix	140-159	20
β-strand	162-163	2	3
α-helix	169-171	3
β-strand	172-174	3	2
β-strand	180-182	3	2
β-strand	189-190	2	3
β-strand	195	1	4
β-strand	200	1	5
α-helix	202-204	3
α-helix	207-210	4
β-strand	215	1	4
α-helix	218-233	16
α-helix	243-251	9
α-helix	263-272	10
α-helix	277-279	3
α-helix	289-292	4
α-helix	295-297	3
α-helix	302-306	5
α-helix	311-312	2
α-helix	345-347	3

Chain I: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	6-12	7
α-helix	18-21	4
β-strand	22	1	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cAMP-dependent protein kinase, alpha-catalytic subunit	E	protein	351	Mus musculus	P05132 (AlphaFold model)
cAMP-dependent protein kinase inhibitor, alpha form	I	protein	20		P61926 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>2ERZ_1 cAMP-dependent protein kinase, alpha-catalytic subunit (chains E)
MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVML
VKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF

Sequence of entity 2 (I), FASTA

>2ERZ_2 cAMP-dependent protein kinase inhibitor, alpha form (chains I)
TTYADFIASGRTGRRNAIHD

Ligands and cofactors

ID	Name	Formula	Copies
HFS	1-(1-hydroxy-5-isoquinolinesulfonyl)homopiperazine	C14 H17 N3 O3 S	1

Primary citation

The Structure of Dimeric ROCK I Reveals the Mechanism for Ligand Selectivity. Jacobs, M., Hayakawa, K., Swenson, L. et al. J Biol Chem (2006) 281:260-268. DOI 10.1074/jbc.M508847200 · PubMed

Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RDQ 1.26 Å, Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
4DFX 1.35 Å, Crystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein…
4HPU 1.55 Å, Crystal structure of the catalytic subunit of cAMP-dependent protein kinase displaying…
4IAI 1.55 Å, X-ray Structure of cAMP dependent protein kinase A in complex with high Ca2+…
9PC1 1.55 Å, Co-crystal structure of the cAMP-dependent protein kinase catalytic subunit alpha with…
3FJQ 1.6 Å, Crystal structure of cAMP-dependent protein kinase catalytic subunit alpha in complex…
4IAK 1.6 Å, Low temperature X-ray structure of cAMP dependent protein kinase A in complex with high…
3IDB 1.62 Å, Crystal structure of (108-268)RIIb:C holoenzyme of cAMP-dependent protein kinase
4IB1 1.63 Å, Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP…
7V0G 1.63 Å, Structure of cAMP-dependent protein kinase using a MD-MX procedure, produced using 1.63…
3QAL 1.7 Å, Crystal Structure of Arg280Ala mutant of Catalytic subunit of cAMP-dependent Protein…
3X2W 1.7 Å, Michaelis complex of cAMP-dependent Protein Kinase Catalytic Subunit

Browse structure collections

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