2A27: Death-associated protein kinase 2

Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the asymmetric unit. Determined by X-ray diffraction at 3.0 Å resolution. Released 10 Oct 2006.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 20,003
Mol. weight: 297.44 kDa
Ligands: DTT
Released: 10 Oct 2006

Explore 2A27 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A27 contains 127 α-helices and 142 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, 17 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	1
α-helix	9-12	4
β-strand	13-18	6	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	73	1	3
β-strand	76	1	3
β-strand	79-84	6	1
β-strand	88-94	7	1
β-strand	100	1	3
α-helix	101-105	5
β-strand	112	1	4
α-helix	113-132	20
β-strand	135-136	2	5
β-strand	145-147	3	3
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	293-302	10

Chain B: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	6
α-helix	9-11	3
β-strand	13-18	6	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	58-68	11
β-strand	73	1	8
β-strand	76	1	8
β-strand	79-84	6	6
β-strand	88-94	7	6
β-strand	100	1	8
α-helix	101-107	7
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	197-212	16
α-helix	222-231	10
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: 17 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	11
α-helix	9-12	4
β-strand	13-18	6	11
β-strand	25-32	8	11
β-strand	38-45	8	11
α-helix	46	1
α-helix	58-70	13
β-strand	73	1	12
β-strand	76	1	12
β-strand	79-84	6	11
β-strand	88-93	6	11
β-strand	100	1	12
α-helix	101-105	5
β-strand	112	1	13
α-helix	113-132	20
β-strand	135-136	2	14
α-helix	142-144	3
β-strand	145-147	3	12
β-strand	157-159	3	12
β-strand	166-167	2	14
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	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	13
α-helix	293-301	9

Chain D: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	15
α-helix	9-12	4
β-strand	13-18	6	15
β-strand	25-32	8	15
β-strand	38-45	8	15
β-strand	46	1	16
α-helix	47	1
β-strand	56	1	16
α-helix	58-70	13
β-strand	73	1	17
β-strand	76	1	17
β-strand	79-84	6	15
β-strand	88-94	7	15
β-strand	100	1	17
α-helix	101-107	7
β-strand	112	1	18
α-helix	113-132	20
β-strand	135-136	2	19
α-helix	142-144	3
β-strand	145-147	3	17
α-helix	155-156	2
β-strand	157-159	3	17
β-strand	166-167	2	19
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	246-253	8
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	18
α-helix	293-302	10

Chain E: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	20
α-helix	9-12	4
β-strand	13	1	21
β-strand	18-21	4	20
β-strand	25-31	7	20
β-strand	32	1	21
β-strand	38-45	8	20
β-strand	46	1	22
β-strand	56	1	22
α-helix	58-70	13
β-strand	73	1	23
β-strand	76	1	23
β-strand	79-84	6	20
β-strand	88-94	7	20
β-strand	100	1	23
α-helix	101-107	7
β-strand	112	1	24
α-helix	113-132	20
β-strand	135-136	2	25
α-helix	142-144	3
β-strand	145-147	3	23
β-strand	157-159	3	23
β-strand	166-167	2	25
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	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	24
α-helix	293-301	9

Chain F: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	26
α-helix	9-12	4
β-strand	13	1	27
β-strand	18	1	26
β-strand	25-31	7	26
β-strand	32	1	27
β-strand	38-45	8	26
β-strand	46	1	28
α-helix	47	1
β-strand	56	1	28
α-helix	58-70	13
β-strand	73	1	29
β-strand	76	1	29
β-strand	79-84	6	26
β-strand	88-94	7	26
β-strand	100	1	29
α-helix	101-107	7
β-strand	112	1	30
α-helix	113-132	20
β-strand	135-136	2	31
α-helix	142-144	3
β-strand	145-147	3	29
β-strand	157-159	3	29
β-strand	166-167	2	31
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	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	30
α-helix	293-302	10

Chain G: 16 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	32
α-helix	9-12	4
β-strand	13	1	33
β-strand	18-21	4	32
β-strand	25-31	7	32
β-strand	32	1	33
β-strand	38-45	8	32
β-strand	46	1	34
β-strand	56	1	34
α-helix	58-70	13
β-strand	73	1	35
β-strand	76	1	35
β-strand	79-84	6	32
β-strand	88-94	7	32
α-helix	95	1
β-strand	100	1	35
α-helix	101-106	6
β-strand	112	1	36
α-helix	113-132	20
β-strand	135-136	2	37
β-strand	145-147	3	35
β-strand	157-159	3	35
β-strand	166-167	2	37
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	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	36
α-helix	293-301	9

Chain H: 15 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	38
α-helix	9-12	4
β-strand	13	1	39
β-strand	18	1	38
β-strand	27-31	5	38
β-strand	32	1	39
β-strand	38-45	8	38
β-strand	46	1	40
β-strand	56	1	40
α-helix	58-70	13
β-strand	73	1	41
β-strand	76	1	41
β-strand	79-84	6	38
β-strand	88-94	7	38
β-strand	100	1	41
α-helix	101-106	6
β-strand	112	1	42
α-helix	113-132	20
β-strand	135-136	2	43
β-strand	145-147	3	41
β-strand	157-159	3	41
β-strand	166-167	2	43
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	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	42
α-helix	293-301	9

Molecules and chains

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

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>2A27_1 Death-associated protein kinase 2 (chains A, B, C, D, E, F, G, H)
GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE
EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF
IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG
TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEE
FFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQ
YVRRRSKLAFSIVSLCNHLTR

Ligands and cofactors

ID	Name	Formula	Copies
DTT	2,3-dihydroxy-1,4-dithiobutane	C4 H10 O2 S2	8

Primary citation

Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the asymmetric unit. Kursula, P., Lehmann, F., Shani, G. et al. 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
6PAW 2.95 Å, Crystal structure of DAPK2 S308A Calcium/Calmodulin complex
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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