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6KL8

Crystal structure of Piptidyl t-RNA hydrolase from Acinetobacter baumannii with bound NaCl at the substrate binding site

Functional Information from GO Data
ChainGOidnamespacecontents
A0004045molecular_functionaminoacyl-tRNA hydrolase activity
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 201
ChainResidue
AASN12
AHIS22
AASN116
ANA202

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 202
ChainResidue
AMET69
AASN70
ACL201

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 203
ChainResidue
AGLY114
AHIS115
AASN116
AHOH318
AHIS22
ALEU97

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YaqTRHNaGfwFVE
ChainResidueDetails
ATYR17-GLU30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLRDI
ChainResidueDetails
AGLY111-ILE121

227344

PDB entries from 2024-11-13

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