Research workbench

Apo CAKIP3[2-436]-L2-MUTANT(HSKHC) in complex with a microtubule

Analyse Apo CAKIP3[2-436]-L2-MUTANT(HSKHC) 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: 7TR2
Type: protein
Length: 1,207 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: C4YNU9, P33176, Q2XVP4, A0A287AGU7
Ligands: GTP, GDP, TA1, MG

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
K	—	protein	338	—	C4YNU9, P33176
A	—	protein	440	—	Q2XVP4
B	—	protein	429	—	A0A287AGU7

Ligands and binding sites

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

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

Compared structures

7TR2 · Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule · the same entry in another collection · chain K against K, TM-score 1.00
P33176 · AlphaFold monomer V2.0 prediction for kinesin-1 heavy chain (P33176) · a predicted model of the same protein · chain K against A, TM-score 0.84

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 C4YNU9
Every structure of UniProt P33176
Every structure of UniProt Q2XVP4
Every structure of UniProt A0A287AGU7
Elsewhere: RCSB PDB 7TR2 · PDBe 7TR2 · UniProt C4YNU9 · UniProt P33176 · UniProt Q2XVP4 · UniProt A0A287AGU7

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