1WMK: Death-associated protein kinase 2

Human death-associated kinase DRP-1, mutant S308D d40. Determined by X-ray diffraction at 3.6 Å resolution. Released 31 Jan 2006.

Method: X-ray diffraction
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 8
Atoms: 19,951
Mol. weight: 297.35 kDa
Released: 31 Jan 2006

Explore 1WMK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1WMK contains 115 α-helices and 137 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: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	13	1	2
β-strand	20-21	2	1
β-strand	25-31	7	1
β-strand	32	1	2
β-strand	38-45	8	1
β-strand	46	1	3
α-helix	47	1
β-strand	56	1	3
α-helix	58-70	13
β-strand	79-84	6	1
β-strand	88-93	6	1
β-strand	100	1	4
α-helix	101-107	7
β-strand	112	1	5
α-helix	113-132	20
β-strand	135-137	3	6
β-strand	145-147	3	4
β-strand	157-159	3	4
α-helix	162-164	3
β-strand	165-167	3	6
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	5
α-helix	293-301	9

Chain B: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	19
α-helix	9-12	4
β-strand	13	1	20
β-strand	18	1	19
β-strand	25-31	7	19
β-strand	32	1	20
β-strand	38-45	8	19
β-strand	46	1	21
α-helix	47	1
β-strand	56	1	21
α-helix	58-69	12
β-strand	79-84	6	19
β-strand	88-93	6	19
β-strand	100	1	22
α-helix	101-107	7
β-strand	112	1	23
α-helix	113-132	20
β-strand	135-137	3	24
β-strand	145-147	3	22
α-helix	155-156	2
β-strand	157-159	3	22
α-helix	162-164	3
β-strand	165-167	3	24
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	23
α-helix	293-301	9

Chain C: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	13
β-strand	13	1	14
β-strand	18-21	4	13
β-strand	25-31	7	13
β-strand	32	1	14
β-strand	38-45	8	13
β-strand	46	1	15
α-helix	47	1
β-strand	56	1	15
α-helix	58-69	12
β-strand	76	1	16
β-strand	79-84	6	13
β-strand	88-93	6	13
β-strand	100	1	16
α-helix	101-107	7
β-strand	112	1	17
α-helix	113-132	20
β-strand	135-137	3	18
β-strand	145-147	3	16
α-helix	155-156	2
β-strand	157-159	3	16
α-helix	162-164	3
β-strand	165-167	3	18
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	17
α-helix	293-301	9

Chain D: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	31
β-strand	13	1	32
β-strand	18	1	31
β-strand	25-31	7	31
β-strand	32	1	32
β-strand	38-45	8	31
β-strand	46	1	33
α-helix	47	1
β-strand	56	1	33
α-helix	58-69	12
β-strand	79-84	6	31
β-strand	88-93	6	31
β-strand	100	1	34
α-helix	101-107	7
β-strand	112	1	35
α-helix	113-132	20
β-strand	135-137	3	36
β-strand	145-147	3	34
α-helix	155-156	2
β-strand	157-159	3	34
α-helix	162-164	3
β-strand	165-167	3	36
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	35
α-helix	293-301	9

Chains E and G: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	7
β-strand	13	1	8
β-strand	18-21	4	7
β-strand	25-31	7	7
β-strand	32	1	8
β-strand	38-45	8	7
β-strand	46	1	9
α-helix	47	1
β-strand	56	1	9
α-helix	58-70	13
β-strand	79-84	6	7
β-strand	88-93	6	7
β-strand	100	1	10
α-helix	101-107	7
β-strand	112	1	11
α-helix	113-132	20
β-strand	135-137	3	12
β-strand	145-147	3	10
α-helix	155-156	2
β-strand	157-159	3	10
α-helix	162-164	3
β-strand	165-167	3	12
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	11
α-helix	293-301	9
α-helix	309-313	5

Chain F: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	25
α-helix	9-12	4
β-strand	13	1	26
β-strand	18	1	25
β-strand	25-31	7	25
β-strand	32	1	26
β-strand	38-45	8	25
β-strand	46	1	27
α-helix	47	1
β-strand	56	1	27
α-helix	58-70	13
β-strand	79-84	6	25
β-strand	88-93	6	25
β-strand	100	1	28
α-helix	101-107	7
β-strand	112	1	29
α-helix	113-132	20
β-strand	135-137	3	30
β-strand	145-147	3	28
α-helix	155-156	2
β-strand	157-159	3	28
α-helix	162-164	3
β-strand	165-167	3	30
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	29
α-helix	293-301	9

Chain H: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	37
α-helix	9-12	4
β-strand	13	1	38
β-strand	18-21	4	37
β-strand	25-31	7	37
β-strand	32	1	38
β-strand	38-45	8	37
β-strand	46	1	39
α-helix	47	1
β-strand	56	1	39
α-helix	58-69	12
β-strand	79-84	6	37
β-strand	88-93	6	37
β-strand	100	1	40
α-helix	101-107	7
β-strand	112	1	41
α-helix	113-132	20
β-strand	135-137	3	42
β-strand	145-147	3	40
β-strand	157-159	3	40
α-helix	162-164	3
β-strand	165-167	3	42
α-helix	186-189	4
α-helix	197-211	15
α-helix	222-231	10
α-helix	246-255	10
α-helix	264-265	2
α-helix	266-270	5
α-helix	280-287	8
β-strand	290	1	41
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

>1WMK_1 Death-associated protein kinase 2 (chains A, B, C, D, E, F, G, H)
GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE
EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF
IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG
TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEE
FFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQ
YVRRRWKLDFSIVSLCNHLTR

Primary citation

Structure of the inhibited conformation of DRP-1 kinase. Kursula, P., Shani, G., Kimchi, A. 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
2A27 3.0 Å, Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 8 monomers in the…
1Z9X 3.93 Å, Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 3 monomers in the…

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