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Structure of C-terminally truncated CDC123 from schizosaccharomyces pombe

Analyse Structure of C-terminally truncated CDC123 from schizosaccharomyces pombe in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZGO
Type: protein
Length: 502 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division cycle protein 123
UniProt: Q9P7N5
Pockets: 4 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division cycle protein 123	protein	252	34% helix, 20% strand	Q9P7N5
B	Cell division cycle protein 123	protein	250	32% helix, 20% strand	Q9P7N5

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	711	0.79	0.83	61	empty
2	491	0.72	0.81	48	empty
3	70	0.30	0.74	18	empty
4	63	0.29	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 1037 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

4ZGO · Structure of C-terminally truncated Cdc123 from Schizosaccharomyces pombe · the same entry in another collection · chain A against A, TM-score 1.00
Q9P7N5 · AlphaFold monomer V2.0 prediction for cell division cycle protein 123 (Q9P7N5) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9P7N5
Elsewhere: RCSB PDB 4ZGO · PDBe 4ZGO · UniProt Q9P7N5

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