MolNFT v1 · #190279 · protein

Crystal structure of full-length kinesin-3 klp-6

7WRG · Kinesin-like protein: “Crystal structure of full-length kinesin-3 klp-6”. X-ray diffraction, 2 ligands (ADP, MG), 20 pockets (best druggability 0.82). MolNFT v1 #190279 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7WRG
Type: protein
Length: 1,595 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein
UniProt: G5EFQ4
Ligands: ADP, MG
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein	protein	812	31% helix, 29% strand	G5EFQ4
B	Kinesin-like protein	protein	783	30% helix, 29% strand	G5EFQ4

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1046	0.82	0.83	90	ADP, MG
2	987	0.82	0.83	102	ADP, MG
3	1042	0.80	0.81	89	empty
4	963	0.77	0.79	70	empty
5	374	0.63	0.78	43	empty

Interfaces

1 interface between chains.

A–B · 245 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

7WRG · Crystal structure of full-length kinesin-3 KLP-6 · 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 G5EFQ4
Elsewhere: RCSB PDB 7WRG · PDBe 7WRG · UniProt G5EFQ4

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