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4LWQ

Crystal structure of native peptidyl t-RNA hydrolase from Acinetobacter baumannii at 1.38A 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 Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AGLY14
APHE26
AGLU30
AMET66
AHOH305
AHOH379
AHOH448

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
AGLN31
AGLN158
AHOH472
AHOH477
AHOH486
AGLN19
ATRP27

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

220472

PDB entries from 2024-05-29

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