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EG5-2

Analyse EG5-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A28
Type: protein
Length: 654 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein KIF11
UniProt: P52732
Ligands: ADP, MG
Pockets: 5 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein KIF11	protein	332	35% helix, 27% strand	P52732
B	Kinesin-like protein KIF11	protein	322	34% helix, 31% strand	P52732

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1011	0.80	0.82	106	ADP, MG
2	239	0.57	0.79	27	empty
3	176	0.50	0.77	23	empty
4	65	0.49	0.85	20	empty
5	122	0.48	0.79	22	empty

Interfaces

1 interface between chains.

A–B · 920 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

4A28 · Eg5-2 · the same entry in another collection · chain A against A, TM-score 1.00

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
Elsewhere: RCSB PDB 4A28 · PDBe 4A28 · UniProt P52732

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