Research workbench

KIF14[391-735] - ADP-alfx in complex with a microtubule

Analyse KIF14[391-735] - ADP-alfx in complex with a microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WWU
Type: protein
Length: 1,216 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q2XVP4, A0A287AGU7, L0N7N1
Ligands: GTP, GDP, TA1, ADP, MG

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	440	—	Q2XVP4
B	—	protein	431	—	A0A287AGU7
K	—	protein	345	—	L0N7N1

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · chains A, B
GDP · Guanosine-5'-diphosphate · ligand · chains B
TA1 · Taxol · ligand · chains B
ADP · Adenosine-5'-diphosphate · ligand · chains K
MG · Magnesium ion · metal · chains A, B

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

Compared structures

6WWU · KIF14[391-735] - ADP-AlFx in complex with a microtubule · the same entry in another collection · chain A against A, TM-score 1.00
L0N7N1 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF14 (L0N7N1) · a predicted model of the same protein · chain K against A, TM-score 0.90

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 Q2XVP4
Every structure of UniProt A0A287AGU7
Every structure of UniProt L0N7N1
Elsewhere: RCSB PDB 6WWU · PDBe 6WWU · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt L0N7N1

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