MolNFT v1 · #168971 · protein

KIF14[391-748] - AMP-pnp in complex with a microtubule

6WWO: “KIF14[391-748] - AMP-pnp in complex with a microtubule”. Electron microscopy, 5 ligands (GTP, GDP, TA1). MolNFT v1 #168971 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6WWO
Type: protein
Length: 1,230 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q2XVP4, A0A287AGU7, L0N7N1
Ligands: GTP, GDP, TA1, ANP, MG

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	440	—	Q2XVP4
B	—	protein	429	—	A0A287AGU7
K	—	protein	361	—	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
ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains K
MG · Magnesium ion · metal · 2 copies · chains A, K

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

Compared structures

6WWO · KIF14[391-748] - AMP-PNP 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 0.94

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 6WWO · PDBe 6WWO · UniProt Q2XVP4 · UniProt A0A287AGU7 · UniProt L0N7N1

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