MolNFT v1 · #127995 · protein

Microtubule-bound MKLP2 motor domain in the presence of ADP

5ND2: “Microtubule-bound MKLP2 motor domain in the presence of ADP”. Electron microscopy, 5 ligands (ADP, GTP, GDP). MolNFT v1 #127995 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5ND2
Type: protein
Length: 1,118 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P97329, F2Z4C1, Q6B856
Ligands: ADP, GTP, GDP, TA1, MG

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	—	protein	280	—	P97329
A	—	protein	412	—	F2Z4C1
B	—	protein	426	—	Q6B856

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains C
GTP · Guanosine-5'-triphosphate · ligand · chains A, B
GDP · Guanosine-5'-diphosphate · ligand · chains B
TA1 · Taxol · ligand · chains B
MG · Magnesium ion · metal · 2 copies · chains C, A

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

Compared structures

5ND2 · Microtubule-bound MKLP2 motor domain in the presence of ADP · the same entry in another collection · chain C against C, TM-score 1.00
P97329 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF20A (P97329) · a predicted model of the same protein · chain C against A, TM-score 0.92

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 P97329
Every structure of UniProt F2Z4C1
Every structure of UniProt Q6B856
Elsewhere: RCSB PDB 5ND2 · PDBe 5ND2 · UniProt P97329 · UniProt F2Z4C1 · UniProt Q6B856

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