MolNFT v1 · #126109 · protein

Nucleotide-free kinesin-1 motor domain, P212121 crystal form

5LT0 · Kinesin-like protein: “Nucleotide-free kinesin-1 motor domain, P212121 crystal form”. X-ray diffraction, 2 ligands (SR, SO4), 3 pockets (best druggability 0.43). MolNFT v1 #126109 on GenesisL1: 3D structure, binding sites and…

PDB: 5LT0
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein
UniProt: Q6P164
Ligands: SR, SO4
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein	protein	303	33% helix, 29% strand	Q6P164

Ligands and binding sites

SR · Strontium ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.43	0.81	16	ACT
2	103	0.40	0.77	24	SO4
3	51	0.31	0.77	15	empty

Compared structures

5LT0 · nucleotide-free kinesin-1 motor domain, P212121 crystal form · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6P164
Elsewhere: RCSB PDB 5LT0 · PDBe 5LT0 · UniProt Q6P164

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