6PAW: DAPK2 S308A Calcium/Calmodulin complex

Crystal structure of DAPK2 S308A Calcium/Calmodulin complex. Determined by X-ray diffraction at 2.95 Å resolution. Released 17 Jun 2020.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: Homo sapiens
Chains: 8
Atoms: 12,988
Mol. weight: 217.27 kDa
Ligands: CA
Released: 17 Jun 2020

Explore 6PAW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6PAW contains 87 α-helices and 73 β-strands across 8 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: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	13-21	9	1
β-strand	25-32	8	1
β-strand	38-45	8	1
β-strand	46	1	2
β-strand	56	1	2
α-helix	58-70	13
β-strand	76	1	3
β-strand	79-84	6	1
β-strand	88-94	7	1
β-strand	100	1	3
α-helix	101-106	6
β-strand	112	1	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	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-288	9
β-strand	290	1	4
α-helix	294-317	24

Chain B: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	6
α-helix	9-11	3
β-strand	13-20	8	6
β-strand	25-32	8	6
β-strand	38-45	8	6
β-strand	46	1	7
β-strand	56	1	7
α-helix	58-70	13
β-strand	76	1	8
β-strand	79-84	6	6
β-strand	88-94	7	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
β-strand	157-159	3	8
β-strand	166-167	2	10
α-helix	181-183	3
α-helix	186-189	4
α-helix	192-194	3
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	266-270	5
α-helix	280-288	9
β-strand	290	1	9
α-helix	294-317	24

Chain C: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	70-79	10
α-helix	82-93	12
β-strand	101	1	24
α-helix	103-113	11
α-helix	119-129	11
β-strand	137	1	24
α-helix	139-145	7

Chain D: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	6-20	15
β-strand	28	1	11
α-helix	30-39	10
α-helix	46-54	9
β-strand	64	1	11
α-helix	66-78	13
α-helix	82-93	12
β-strand	101	1	12
α-helix	103-113	11
α-helix	119-129	11
β-strand	137	1	12
α-helix	139-146	8

Chain E: 19 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	13
α-helix	9-12	4
β-strand	13-21	9	13
β-strand	25-32	8	13
β-strand	38-45	8	13
β-strand	46	1	14
β-strand	56	1	14
α-helix	58-70	13
β-strand	76	1	15
α-helix	77-78	2
β-strand	79-84	6	13
β-strand	88-94	7	13
β-strand	100	1	15
α-helix	101-106	6
β-strand	112	1	16
α-helix	113-132	20
β-strand	135-136	2	17
α-helix	142-144	3
β-strand	145-147	3	15
α-helix	155-156	2
β-strand	157-159	3	15
β-strand	166-167	2	17
α-helix	181-183	3
α-helix	186-189	4
α-helix	192-194	3
α-helix	197-212	16
α-helix	222-231	10
α-helix	238-241	4
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-288	9
β-strand	290	1	16
α-helix	293-296	4
α-helix	298-307	10

Chain F: 16 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	18
α-helix	9-11	3
β-strand	13-14	2	18
β-strand	18-21	4	18
β-strand	25-32	8	18
β-strand	38-45	8	18
β-strand	46	1	19
α-helix	47	1
β-strand	56	1	19
α-helix	58-70	13
β-strand	76	1	20
β-strand	79-84	6	18
β-strand	88-94	7	18
β-strand	100	1	20
α-helix	101-105	5
β-strand	112	1	21
α-helix	113-132	20
β-strand	135-136	2	22
α-helix	142-144	3
β-strand	145-147	3	20
α-helix	155-156	2
β-strand	157-159	3	20
β-strand	166-167	2	22
α-helix	181-183	3
α-helix	186-189	4
α-helix	197-212	16
α-helix	222-231	10
α-helix	238-241	4
α-helix	246-255	10
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	21
α-helix	294-315	22

Chain G: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	82-93	12
β-strand	101	1	23
α-helix	103-112	10
α-helix	123-129	7
β-strand	137	1	23
α-helix	139-146	8

Chain H: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	83-90	8
α-helix	105-112	8
α-helix	119-128	10
α-helix	139-146	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Death-associated protein kinase 2	A, B, E, F	protein	323	Homo sapiens	Q9UIK4 (AlphaFold model)
Calmodulin-1	C, D, G, H	protein	149	Homo sapiens	P0DP23 (AlphaFold model)

Sequence of entity 1 (A, B, E, F), FASTA

>6PAW_1 Death-associated protein kinase 2 (chains A, B, E, F)
GHMSEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVS
REEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEAT
SFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNI
FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFD
EEFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFR
KQYVRRRWKLAFSIVSLCNHLTR

Sequence of entity 2 (C, D, G, H), FASTA

>6PAW_2 Calmodulin-1 (chains C, D, G, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	9

Primary citation

Crystal structure of Death-associated protein kinase 2 in complex with Calcium Calmodulin. Simon, B., Wilmanns, M. To be published.

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

2A2A 1.47 Å, High-resolution crystallographic analysis of the autoinhibited conformation of a human…
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
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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