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X-ray crystal structure of protein PSPTO5229 from pseudomonas syringae. northeast structural genomics consortium target PSR62

Analyse X-ray crystal structure of protein PSPTO5229 from pseudomonas syringae.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EVE
Type: protein
Length: 149 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein PSPTO5229
UniProt: Q87UR7
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein PSPTO5229	protein	149	28% helix, 34% strand	Q87UR7

Ligands and binding sites

MPO · 3[N-morpholino]propane sulfonic acid · additive · chains A
EDO · 1,2-ethanediol · additive · chains A
144 · Tris-hydroxymethyl-methyl-ammonium · additive · 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	120	0.43	0.77	20	MPO

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

2EVE · X-Ray Crystal Structure of Protein PSPTO5229 from Pseudomonas syringae. Northeast… · the same entry in another collection · chain A against A, 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 Q87UR7
Elsewhere: RCSB PDB 2EVE · PDBe 2EVE · UniProt Q87UR7

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