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Crystal structure of yeast CDT1 (N terminal and middle domain), form 2.

Analyse Crystal structure of yeast CDT1 (N terminal and middle domain), form 2. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MEA
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division cycle protein CDT1
UniProt: P47112
Ligands: SO4
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division cycle protein CDT1	protein	386	40% helix, 19% strand	P47112

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	175	0.55	0.80	39	GOL
2	66	0.38	0.78	17	empty
3	57	0.38	0.79	13	empty

Compared structures

5MEA · Crystal structure of yeast Cdt1 (N terminal and middle domain), form 2. · the same entry in another collection · chain A against A, TM-score 1.00
P47112 · AlphaFold monomer V2.0 prediction for cell division cycle protein CDT1 (P47112) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P47112
Elsewhere: RCSB PDB 5MEA · PDBe 5MEA · UniProt P47112

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