1ZWS: Catalytic domain of human DRP-1 kinase

Crystal structure of the catalytic domain of human DRP-1 kinase. Determined by X-ray diffraction at 2.9 Å resolution. Released 24 Oct 2006.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 18,024
Mol. weight: 264.77 kDa
Released: 24 Oct 2006

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

Secondary structure: helices and β-sheets

1ZWS contains 108 α-helices and 120 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: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
α-helix	9-12	4
β-strand	13	1	1
β-strand	18-20	3	1
β-strand	25-32	8	1
β-strand	37-44	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	89-93	5	1
α-helix	94-95	2
β-strand	100	1	3
α-helix	101-107	7
α-helix	113-133	21
β-strand	135-136	2	4
α-helix	142-144	3
β-strand	145-147	3	3
β-strand	157-159	3	3
β-strand	166-167	2	4
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain B: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	5
α-helix	9-12	4
β-strand	13	1	5
β-strand	18-20	3	5
β-strand	25-32	8	5
β-strand	37-44	8	5
β-strand	46	1	6
β-strand	56	1	6
α-helix	58-70	13
β-strand	76	1	7
β-strand	79-84	6	5
β-strand	89-93	5	5
β-strand	100	1	7
α-helix	101-107	7
α-helix	113-132	20
β-strand	135-136	2	8
α-helix	142-144	3
β-strand	145-147	3	7
β-strand	157-159	3	7
β-strand	166-167	2	8
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain C: 12 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	9
α-helix	9-11	3
β-strand	13	1	9
β-strand	18-20	3	9
β-strand	25-32	8	9
β-strand	37-44	8	9
β-strand	46	1	10
β-strand	56	1	10
α-helix	58-70	13
β-strand	76	1	11
β-strand	79-84	6	9
β-strand	89-93	5	9
β-strand	99-100	2	11
α-helix	101-107	7
α-helix	113-132	20
β-strand	135-136	2	12
α-helix	142-144	3
β-strand	145-147	3	11
β-strand	157-159	3	11
β-strand	166-167	2	12
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

Chain D: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	13
α-helix	9-12	4
β-strand	13	1	13
β-strand	18-20	3	13
β-strand	25-32	8	13
β-strand	37-44	8	13
β-strand	46	1	14
β-strand	56	1	14
α-helix	58-70	13
β-strand	76	1	15
β-strand	79-84	6	13
β-strand	89-93	5	13
β-strand	100	1	15
α-helix	101-107	7
α-helix	113-133	21
β-strand	135-136	2	16
α-helix	142-144	3
β-strand	145-147	3	15
β-strand	157-159	3	15
β-strand	166-167	2	16
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain E: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	17
α-helix	9-12	4
β-strand	13	1	17
β-strand	18-20	3	17
β-strand	25-32	8	17
β-strand	37-44	8	17
β-strand	46	1	18
β-strand	56	1	18
α-helix	58-70	13
β-strand	76	1	19
β-strand	79-84	6	17
β-strand	89-93	5	17
α-helix	94-96	3
β-strand	99-100	2	19
α-helix	101-107	7
α-helix	113-132	20
β-strand	135-136	2	20
α-helix	142-144	3
β-strand	145-147	3	19
β-strand	157-159	3	19
β-strand	166-167	2	20
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain F: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	21
α-helix	9-12	4
β-strand	13	1	21
β-strand	18-20	3	21
β-strand	25-32	8	21
β-strand	37-44	8	21
β-strand	46	1	22
β-strand	56	1	22
α-helix	58-70	13
β-strand	76	1	23
β-strand	79-84	6	21
β-strand	89-93	5	21
β-strand	100	1	23
α-helix	101-107	7
α-helix	113-132	20
β-strand	135-136	2	24
α-helix	142-144	3
β-strand	145-147	3	23
β-strand	157-159	3	23
β-strand	166-167	2	24
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain G: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	25
α-helix	9-12	4
β-strand	13	1	25
β-strand	18-20	3	25
β-strand	25-32	8	25
β-strand	37-44	8	25
β-strand	46	1	26
β-strand	56	1	26
α-helix	58-70	13
β-strand	76	1	27
β-strand	79-84	6	25
β-strand	89-93	5	25
α-helix	94-96	3
β-strand	100	1	27
α-helix	101-107	7
α-helix	113-133	21
β-strand	135-136	2	28
α-helix	142-144	3
β-strand	145-147	3	27
β-strand	157-159	3	27
β-strand	166-167	2	28
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Chain H: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	29
α-helix	9-12	4
β-strand	13	1	29
β-strand	18-20	3	29
β-strand	25-32	8	29
β-strand	37-45	9	29
β-strand	46	1	30
β-strand	56	1	30
α-helix	58-70	13
β-strand	76	1	31
β-strand	79-84	6	29
β-strand	88-93	6	29
α-helix	94-96	3
β-strand	100	1	31
α-helix	101-107	7
α-helix	113-133	21
β-strand	135-136	2	32
α-helix	142-144	3
β-strand	145-147	3	31
β-strand	157-159	3	31
β-strand	166-167	2	32
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	260-262	3
α-helix	264-265	2
α-helix	266-270	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DAP-kinase related protein 1	A, B, C, D, E, F, G, H	protein	288	Homo sapiens	Q9UIK4 (AlphaFold model)

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

>1ZWS_1 DAP-kinase related protein 1 (chains A, B, C, D, E, F, G, H)
GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE
EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF
IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG
TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFDEE
FFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRR

Primary citation

Crystal structure of the catalytic domain of human DRP-1 kinase. Kursula, P., Schunck, H., 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
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 1ZWS 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.