MolNFT v2 · #124139 · protein

The neck-linker and alpha 7 helix of Homo sapiens Eg5 fused to EB1

5JV3: “The neck-linker and alpha 7 helix of Homo sapiens Eg5 fused to EB1”. X-ray diffraction at 2.006, 1 ligand (CA). MolNFT v2 #124139 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5JV3
Type: protein
Length: 263 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.006
Source: Homo sapiens
UniProt: P52732, Q15691
Ligands: CA

Structure

x-ray diffraction · resolution 2.006 · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	62	—	P52732, Q15691
B	—	protein	69	—	P52732, Q15691
C	—	protein	64	—	P52732, Q15691
D	—	protein	68	—	P52732, Q15691

Ligands and binding sites

CA · Calcium ion · metal · chains D

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

Compared structures

5JV3 · The neck-linker and alpha 7 helix of homo sapiens EG5 fused to EB1 · the same entry in another collection · chain A against A, TM-score 1.00
Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain B against A, TM-score 0.83
P52732 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF11 (P52732) · a predicted model of the same protein · chain A against A, TM-score 0.72

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 P52732
Every structure of UniProt Q15691
Elsewhere: RCSB PDB 5JV3 · PDBe 5JV3 · UniProt P52732 · UniProt Q15691

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