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Crystal structure of cell division cycle 25C protein isoform a from homo sapiens

Analyse Crystal structure of cell division cycle 25C protein isoform a from homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OP3
Type: protein
Length: 167 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: M-phase inducer phosphatase 3
EC: 3.1.3.48
UniProt: P30307
Ligands: SO4
Pockets: 3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	M-phase inducer phosphatase 3 (EC 3.1.3.48)	protein	167	26% helix, 19% strand	P30307

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.43	0.78	17	empty
2	89	0.42	0.78	16	empty
3	68	0.39	0.79	18	SO4

Compared structures

3OP3 · Crystal Structure of Cell Division Cycle 25C Protein Isoform A from Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
P30307 · AlphaFold monomer V2.0 prediction for M-phase inducer phosphatase 3 (P30307) · 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 P30307
Elsewhere: RCSB PDB 3OP3 · PDBe 3OP3 · UniProt P30307

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