MolNFT v1 · #91823 · protein

Crystal structure of peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.86 a resolution

4FOP: “Crystal structure of peptidyl-tRNA hydrolase from acinetobacter baumannii at 1.86 a resolution”. X-ray diffraction, 1 pocket (best druggability 0.35). MolNFT v1 #91823 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4FOP
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
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-tRNA hydrolase (EC 3.1.1.29)	protein	193	41% helix, 22% strand	D0C9L6

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A
ACT · Acetate ion · 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	71	0.35	0.77	20	empty

Compared structures

4FOP · Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 A… · 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 D0C9L6
Elsewhere: RCSB PDB 4FOP · PDBe 4FOP · UniProt D0C9L6

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