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Crystal structure of a deinococcus radiodurans pte-like lactonase (drpll) mutant Y28L/D71N/E101G/E179D/V235L/L270M

Analyse Crystal structure of a deinococcus radiodurans pte-like lactonase (drpll)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J5N
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotriesterase, putative
UniProt: Q9RVU2
Ligands: CO
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotriesterase, putative	protein	322	47% helix, 15% strand	Q9RVU2

Ligands and binding sites

CO · Cobalt (II) ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	214	0.57	0.79	31	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

4J5N · Crystal Structure of a Deinococcus radiodurans PTE-like lactonase (drPLL) mutant… · 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 Q9RVU2
Elsewhere: RCSB PDB 4J5N · PDBe 4J5N · UniProt Q9RVU2

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