7LXR: Kinesin-like protein at 61F

Kinesin-like protein at 61F (Klp61f) bound to AMPPNP. Determined by X-ray diffraction at 1.74 Å resolution. Released 16 Nov 2022.

Method: X-ray diffraction
Resolution: 1.74 Å
Organism: Drosophila melanogaster
Chains: 2
Atoms: 5,909
Mol. weight: 84.42 kDa
Ligands: MG, ANP
Released: 16 Nov 2022

Explore 7LXR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LXR contains 34 α-helices and 46 β-strands across 2 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: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	19	1	1
α-helix	20	1
β-strand	21-26	6	2
α-helix	27-30	4
α-helix	31-35	5
β-strand	40	1	3
β-strand	42-45	4	4
β-strand	49-53	5	4
β-strand	60-65	6	4
β-strand	68-70	3	2
α-helix	76-83	8
α-helix	85-92	8
β-strand	96-103	8	2
β-strand	104	1	5
α-helix	109-113	5
α-helix	118-120	3
α-helix	133-147	15
β-strand	150-162	13	2
β-strand	165-168	4	2
β-strand	179-182	4	6
β-strand	190-193	4	6
β-strand	198-200	3	2
α-helix	203-216	14
β-strand	219-222	4	7
β-strand	225-229	5	7
β-strand	232-243	12	2
β-strand	252-261	10	2
α-helix	262-264	3
β-strand	265	1	5
α-helix	277-301	25
α-helix	308-310	3
α-helix	312-317	6
α-helix	318-320	3
β-strand	326-333	8	2
β-strand	336	1	3
α-helix	337-339	3
α-helix	340-353	14
α-helix	356	1
β-strand	357	1	1
α-helix	358	1
β-strand	364	1	2

Chain B: 16 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	21-26	6	8
α-helix	27-28	2
α-helix	31-35	5
α-helix	38-39	2
β-strand	40	1	9
β-strand	42-44	3	10
β-strand	49-52	4	10
β-strand	62-65	4	10
β-strand	68-70	3	8
α-helix	76-83	8
α-helix	85-92	8
β-strand	96-103	8	8
β-strand	104	1	11
α-helix	109-113	5
β-strand	115	1	12
α-helix	118-120	3
β-strand	131	1	12
α-helix	133-148	16
β-strand	151-162	12	8
β-strand	165-168	4	8
β-strand	179-181	3	13
β-strand	191-193	3	13
β-strand	198-200	3	8
α-helix	203-216	14
β-strand	219-222	4	14
β-strand	225-229	5	14
β-strand	232-243	12	8
β-strand	251-261	11	8
α-helix	262-264	3
β-strand	265	1	11
α-helix	277-301	25
α-helix	308-310	3
α-helix	312-317	6
α-helix	318-320	3
β-strand	326-333	8	8
β-strand	336	1	9
α-helix	337-339	3
α-helix	340-353	14
β-strand	364-366	3	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein Klp61F	A, B	protein	369	Drosophila melanogaster	P46863 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7LXR_1 Kinesin-like protein Klp61F (chains A, B)
GAMDISGGNTSRQPQKKSNQNIQVYVRVRPLNSRERCIRSAEVVDVVGPREVVTRHTLDS
KLTKKFTFDRSFGPESKQCDVYSVVVSPLIEEVLNGYNCTVFAYGQTGTGKTHTMVGNET
AELKSSWEDDSDIGIIPRALSHLFDELRMMEVEYTMRISYLELYNEELCDLLSTDDTTKI
RIFDDSTKKGSVIIQGLEEIPVHSKDDVYKLLEKGKERRKTATTLMNAQSSRSHTVFSIV
VHIRENGIEGEDMLKIGKLNLVDLAGSENVSKAGNEKGIRVRETVNINQSLLTLGRVITA
LVDRAPHVPYRESKLTRLLQESLGGRTKTSIIATISPGHKDIEETLSTLEYAHRAKNIQN
KPEVNQKLT

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2

Water and common crystallization additives (IOD, EDO) are not listed.

Primary citation

Crystal Structure of the Klp61f motor domain bound to AMPPNP. Wojcik, E.J., Worthylake, D.K. To be published.

Other PDB entries of the same protein (UniProt P46863 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4PXU 2.6 Å, Structural basis for the assembly of the mitotic motor kinesin-5 into bipolar tetramers
4PXT 2.9 Å, Structural basis for the assembly of the mitotic motor kinesin-5 into bipolar tetramers
6VPO 4.4 Å, Cryo-EM structure of microtubule-bound KLP61F motor domain in the AMPPNP state
6VPP 4.4 Å, Cryo-EM structure of microtubule-bound KLP61F motor with tail domain in the…
7S5U 4.41 Å, Extended bipolar assembly domain of kinesin-5 minifilament
2WBE 9.4 Å, Kinesin-5-Tubulin Complex with AMPPNP

Browse structure collections

About this viewer

MolViewer shows 7LXR 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.