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5GVZ

Crystal structure of Peptidyl-tRNA hydrolase from Vibrio cholerae in space group C2221 at resolution 1.75A.

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 Residues5
Detailsbinding site for residue SO4 A 201
ChainResidue
AARG36
AHIS145
ALYS146
AHOH355
AHOH384

site_idAC2
Number of Residues2
Detailsbinding site for residue ACT A 202
ChainResidue
ALEU101
AARG137

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT A 203
ChainResidue
AGLN188
ALYS109
AGLN110

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YakTRHNaGawVVE
ChainResidueDetails
ATYR19-GLU32

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GhggHNGLKDT
ChainResidueDetails
AGLY113-THR123

222415

PDB entries from 2024-07-10

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