3GU6: DAPKQ23V-ADP

Crystal structure of DAPKQ23V-ADP. Determined by X-ray diffraction at 1.49 Å resolution. Released 9 Mar 2010.

Method: X-ray diffraction
Resolution: 1.49 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,677
Mol. weight: 34.32 kDa
Ligands: ADP
Released: 9 Mar 2010

Explore 3GU6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GU6 contains 15 α-helices and 16 β-strands across 1 chain. 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
α-helix	9-11	3
β-strand	13-22	10	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	88-94	7	1
β-strand	100	1	3
α-helix	101-108	8
α-helix	113-132	20
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
β-strand	173	1	5
α-helix	181-183	3
α-helix	186-189	4
β-strand	194	1	5
α-helix	197-212	16
α-helix	222-230	9
α-helix	238-241	4
α-helix	246-253	8
α-helix	260-262	3
α-helix	264-265	2
α-helix	266-271	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Death-associated protein kinase 1	A	protein	295	Homo sapiens	P53355 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3GU6_1 Death-associated protein kinase 1 (chains A)
MTVFRQENVDDYYDTGEELGSGVFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSRED
IEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFL
KQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGT
PEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEY
FSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSSAWSHPQFEK

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1

Primary citation

Enzymatic activity and crystallographic analyses of a glycine-rich loop mutant of DAPK. McNamara, L.K., Schavocky, J.S., Watterson, D.M. et al. To be published.

Other PDB entries of the same protein (UniProt P53355 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6GY5 1.09 Å, Crystal structure of the kelch domain of human KLHL20 in complex with DAPK1 peptide
4PF4 1.13 Å, 1.1A X-ray structure of the apo catalytic domain of death-associated protein kinase 1,…
2W4J 1.3 Å, X-ray structure of a DAP-Kinase 2-277
3GU4 1.35 Å, Crystal structure of DAPKQ23V-AMPPNP
9N2M 1.35 Å, Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound MW01-30-047SRM
4YPD 1.4 Å, Crystal Structure of DAPK1 catalytic domain in complex with the hinge binding fragment…
5AV4 1.4 Å, Crystal structure of DAPK1-genistein complex in the presence of bromide ions.
7CCW 1.4 Å, Crystal structure of death-associated protein kinase 1 in complex with resveratrol and MES
9N1T 1.43 Å, Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound SRM-26-100
9N2O 1.49 Å, Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound MW01-27-040SRM
9O73 1.49 Å, Crystal Structure of Human DAPK1 Catalytic Subunit Complexed with Compound MW01-30-035SRM
1JKS 1.5 Å, 1.5A X-ray structure of apo form of a catalytic domain of death-associated protein kinase

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