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Structure of a C.ELEGANS sex determining protein

Analyse Structure of a C.ELEGANS sex determining protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JND
Type: protein
Length: 408 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CA(2+)/CALMODULIN-dependent protein kinase phosphatase
EC: 3.1.3.16
UniProt: P49594
Ligands: MG
Pockets: 5 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CA(2+)/CALMODULIN-dependent protein kinase phosphatase (EC 3.1.3.16)	protein	408	45% helix, 19% strand	P49594

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

5 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	140	0.54	0.81	27	empty
2	185	0.50	0.77	21	empty
3	72	0.36	0.77	14	empty
4	77	0.35	0.77	15	MG
5	58	0.30	0.75	14	empty

Compared structures

4JND · Structure of a C.elegans sex determining protein · the same entry in another collection · chain A against A, TM-score 1.00
P49594 · AlphaFold monomer V2.0 prediction for protein phosphatase fem-2 (P49594) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P49594
Elsewhere: RCSB PDB 4JND · PDBe 4JND · UniProt P49594

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