2CKE: Human death-associated DRP-1 kinase

Human death-associated DRP-1 kinase in complex with inhibitor. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 May 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 9,904
Mol. weight: 149.67 kDa
Ligands: IQU
Released: 15 May 2007

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

Secondary structure: helices and β-sheets

2CKE contains 77 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: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5	1	1
α-helix	9-11	3
β-strand	13-20	8	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	101-105	5
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	168-169	2
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	4
α-helix	293-298	6

Chain B: 20 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	13-20	8	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	58-68	11
β-strand	76	1	8
β-strand	79-84	6	6
β-strand	88-93	6	6
β-strand	100	1	8
α-helix	101-105	5
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	168-169	2
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	246-253	8
α-helix	264-265	2
α-helix	266-271	6
α-helix	280-288	9
β-strand	290	1	9
α-helix	293-298	6

Chain C: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	3-4	2
β-strand	5	1	11
α-helix	9-11	3
β-strand	13-22	10	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	58-70	13
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	222-231	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	14
α-helix	293-300	8

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	13-21	9	16
β-strand	25-32	8	16
β-strand	38-45	8	16
β-strand	46	1	17
β-strand	56	1	17
α-helix	58-70	13
β-strand	76	1	18
β-strand	79-84	6	16
β-strand	88-94	7	16
β-strand	100	1	18
α-helix	101-105	5
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	186-190	5
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
α-helix	289	1
β-strand	290	1	19
α-helix	291	1
α-helix	293-298	6

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

>2CKE_1 DEATH-ASSOCIATED PROTEIN KINASE 2 (chains A, B, C, D)
GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE
EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF
IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG
TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFDEE
FFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQ
YVRRRWKLSFSIVSLCNHLTR

Ligands and cofactors

ID	Name	Formula	Copies
IQU	N-(2-aminoethyl)isoquinoline-5-sulfonamide	C11 H13 N3 O2 S	4

Primary citation

Crystal Structure of Human Drp-1 Complexed with an Inhibitor. Kursula, P., 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…
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…

Browse structure collections

About this viewer

MolViewer shows 2CKE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.