Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4YLY

Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, staphylococcus aureus at 2.25 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004045molecular_functionaminoacyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
B0004045molecular_functionaminoacyl-tRNA hydrolase activity
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 201
ChainResidue
AARG50
ALYS55
BTYR79
BHOH309

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 202
ChainResidue
AARG50
BTYR78
BTYR79

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 203
ChainResidue
AASP153
AHOH330
ASER151
AASN152

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 204
ChainResidue
AARG103
AGLN104
AMET182
AHOH329

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL B 201
ChainResidue
AARG177
BGLN104
BSER176
BARG177
BPHE178
BASP179

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. FelTRHNiGfeVVD
ChainResidueDetails
APHE14-ASP27

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. SaggHNGMKSI
ChainResidueDetails
ASER107-ILE117

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon