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Crystal structure of na+ bound peptidyl-tRNA hydrolase from acinetobacter baumannii at 2.19 a resolution

Analyse Crystal structure of na+ bound peptidyl-tRNA hydrolase from acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6A31
Type: protein
Length: 193 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-tRNA hydrolase
EC: 3.1.1.29
UniProt: D0C9L6
Ligands: NA
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-tRNA hydrolase (EC 3.1.1.29)	protein	193	40% helix, 22% strand	D0C9L6

Ligands and binding sites

NA · Sodium 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.37	0.78	19	empty

Compared structures

6A31 · Crystal structure of Na+ bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii at… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt D0C9L6
Elsewhere: RCSB PDB 6A31 · PDBe 6A31 · UniProt D0C9L6

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