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Structure of a plant phosphatase

Analyse Structure of a plant phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NME
Type: protein
Length: 579 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SEX4 glucan phosphatase
UniProt: Q944A8
Ligands: PO4
Pockets: 5 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SEX4 glucan phosphatase	protein	290	36% helix, 26% strand	Q944A8
B	SEX4 glucan phosphatase	protein	289	37% helix, 25% strand	Q944A8

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

5 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	933	0.85	0.86	97	PO4
2	219	0.51	0.76	24	empty
3	188	0.48	0.76	25	empty
4	101	0.41	0.77	20	empty
5	100	0.37	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 1199 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

3NME · Structure of a plant phosphatase · the same entry in another collection · chain B against B, TM-score 1.00

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 Q944A8
Elsewhere: RCSB PDB 3NME · PDBe 3NME · UniProt Q944A8

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