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Crystal structure of the polo-box domain of CDC5 from budding yeast.

Analyse Crystal structure of the polo-box domain of CDC5 from budding yeast. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MF4
Type: protein
Length: 235 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell cycle SERINE/THREONINE-protein kinase CDC5/MSD2
EC: 2.7.11.21
UniProt: P32562
Ligands: ZN
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell cycle SERINE/THREONINE-protein kinase CDC5/MSD2 (EC 2.7.11.21)	protein	235	31% helix, 29% strand	P32562

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.37	0.76	20	empty

Compared structures

6MF4 · Crystal structure of the polo-box domain of Cdc5 from budding yeast. · the same entry in another collection · chain A against A, TM-score 1.00
P32562 · AlphaFold monomer V2.0 prediction for cell cycle SERINE/THREONINE- protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P32562
Elsewhere: RCSB PDB 6MF4 · PDBe 6MF4 · UniProt P32562

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