2A2A: Death-associated protein kinase 2

High-resolution crystallographic analysis of the autoinhibited conformation of a human death-associated protein kinase. Determined by X-ray diffraction at 1.47 Å resolution. Released 17 Oct 2006.

Method: X-ray diffraction
Resolution: 1.47 Å
Organism: Homo sapiens
Chains: 4
Atoms: 11,556
Mol. weight: 149.85 kDa
Ligands: DTT
Released: 17 Oct 2006

Explore 2A2A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A2A contains 73 α-helices and 64 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, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	1
α-helix	9-12	4
β-strand	13-21	9	1
β-strand	25-32	8	1
β-strand	38-45	8	1
β-strand	46	1	2
α-helix	47	1
β-strand	56	1	2
α-helix	58-70	13
β-strand	76	1	3
β-strand	79-84	6	1
β-strand	88-93	6	1
β-strand	100	1	3
α-helix	101-106	6
β-strand	111-112	2	4
α-helix	113-132	20
β-strand	135-136	2	5
α-helix	142-144	3
β-strand	145-147	3	3
α-helix	155-156	2
β-strand	157-159	3	3
β-strand	166-167	2	5
α-helix	181-183	3
α-helix	186-189	4
α-helix	197-212	16
α-helix	222-230	9
α-helix	238-241	4
α-helix	246-253	8
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290-291	2	4
α-helix	293-302	10

Chain B: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	6
α-helix	9-12	4
β-strand	13-21	9	6
β-strand	25-32	8	6
β-strand	38-45	8	6
β-strand	46	1	7
α-helix	47	1
β-strand	56	1	7
α-helix	58-70	13
β-strand	76	1	8
β-strand	79-84	6	6
β-strand	88-93	6	6
β-strand	100	1	8
α-helix	101-106	6
β-strand	112	1	9
α-helix	113-132	20
β-strand	135-136	2	10
α-helix	142-144	3
β-strand	145-147	3	8
α-helix	155-156	2
β-strand	157-159	3	8
β-strand	166-167	2	10
α-helix	181-183	3
α-helix	186-189	4
α-helix	197-212	16
α-helix	222-230	9
α-helix	238-241	4
α-helix	246-253	8
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	9
α-helix	293-302	10

Chain C: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	11
α-helix	9-12	4
β-strand	13-20	8	11
β-strand	25-32	8	11
β-strand	38-45	8	11
β-strand	46	1	12
α-helix	47	1
β-strand	56	1	12
α-helix	58-68	11
β-strand	76	1	13
β-strand	79-84	6	11
β-strand	88-94	7	11
β-strand	100	1	13
α-helix	101-105	5
β-strand	112	1	14
α-helix	113-132	20
β-strand	135-136	2	15
α-helix	142-144	3
β-strand	145-147	3	13
α-helix	155-156	2
β-strand	157-159	3	13
β-strand	166-167	2	15
α-helix	181-183	3
α-helix	186-189	4
α-helix	197-212	16
α-helix	222-230	9
α-helix	238-241	4
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	14
α-helix	293-302	10

Chain D: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	16
α-helix	9-12	4
β-strand	13-20	8	16
β-strand	25-32	8	16
β-strand	38-45	8	16
β-strand	46	1	17
α-helix	47	1
β-strand	56	1	17
α-helix	58-70	13
β-strand	76	1	18
β-strand	79-84	6	16
β-strand	88-93	6	16
β-strand	100	1	18
α-helix	101-106	6
β-strand	112	1	19
α-helix	113-132	20
β-strand	135-136	2	20
α-helix	142-144	3
β-strand	145-147	3	18
α-helix	155-156	2
β-strand	157-159	3	18
β-strand	166-167	2	20
α-helix	181-183	3
α-helix	186-189	4
α-helix	197-212	16
α-helix	222-230	9
α-helix	238-241	4
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	19
α-helix	293-300	8
α-helix	301-303	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Death-associated protein kinase 2	A, B, C, D	protein	321	Homo sapiens	Q9UIK4 (AlphaFold model)

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

>2A2A_1 Death-associated protein kinase 2 (chains A, B, C, D)
GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE
EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF
IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG
TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFDEE
FFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQ
YVRRRWKLSFSIVSLCNHLTR

Ligands and cofactors

ID	Name	Formula	Copies
DTT	2,3-dihydroxy-1,4-dithiobutane	C4 H10 O2 S2	4

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

Primary citation

Death-Associated Protein Kinase Activity Is Regulated by Coupled Calcium/Calmodulin Binding to Two Distinct Sites. Simon, B., Huart, A.S., Temmerman, K. et al. Structure (2016). DOI 10.1016/j.str.2016.03.020 · PubMed

Other PDB entries of the same protein (UniProt Q9UIK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ZUZ 1.91 Å, Calmodulin in complex with a mutant peptide from human DRP-1 kinase
1WRZ 2.0 Å, Calmodulin complexed with a peptide from a human death-associated protein kinase
7A6Y 2.5 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide stabilized by FC-A
7A6R 2.7 Å, Structure of 14-3-3 gamma in complex with DAPK2 peptide containing the 14-3-3 binding…
2CKE 2.8 Å, Human death-associated DRP-1 kinase in complex with inhibitor
1ZWS 2.9 Å, Crystal structure of the catalytic domain of human DRP-1 kinase
6PAW 2.95 Å, Crystal structure of DAPK2 S308A Calcium/Calmodulin complex
2A27 3.0 Å, Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the…
1WMK 3.6 Å, Human death-associated kinase DRP-1, mutant S308D d40
1Z9X 3.93 Å, Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 3 monomers in the…

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