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Crystal structure of a putative had-like phosphatase (MLL2559) from mesorhizobium loti at 1.50 a resolution

Analyse Crystal structure of a putative had-like phosphatase (MLL2559) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O2X
Type: protein
Length: 209 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein
UniProt: Q98I56
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein	protein	209	34% helix, 21% strand	Q98I56

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	132	0.49	0.79	25	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2O2X · Crystal structure of a putative had-like phosphatase (mll2559) from mesorhizobium loti at… · the same entry in another collection · chain A against A, TM-score 1.00
Q98I56 · AlphaFold monomer V2.0 prediction for D-glycero-beta-D-manno- heptose-1,7-bisphosphate… · 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 Q98I56
Elsewhere: RCSB PDB 2O2X · PDBe 2O2X · UniProt Q98I56

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