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6JJQ

Crystal structure of peptidyl-tRNA hydrolase from Acinetobacter baumannii at 0.99 A resolution.

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 Residues2
Detailsbinding site for residue PEG A 201
ChainResidue
ALYS35
AHOH429

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 202
ChainResidue
AARG105
AARG133
AHOH347

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
AASN12
AHIS22
AASN116

site_idAC4
Number of Residues5
Detailsbinding site for residue CL A 204
ChainResidue
AARG131
AHOH386
AHOH458
AHOH466
AHIS94

site_idAC5
Number of Residues4
Detailsbinding site for residue NA A 205
ChainResidue
AGLN19
ATRP27
AALA153
AGLN158

site_idAC6
Number of Residues5
Detailsbinding site for residue NA A 206
ChainResidue
ALYS152
AGLN179
APRO181
AGLN182
AHOH345

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

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PDB entries from 2024-07-24

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