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5IVP

Crystal structure of the Peptidyl-tRNA hydrolase from Vibrio cholerae in the C121 space group at pH 6.5

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 Residues7
Detailsbinding site for residue FLC A 201
ChainResidue
AASN14
AHIS24
APHE70
AMET71
AASN72
AASN118
ALEU154

site_idAC2
Number of Residues11
Detailsbinding site for residue FLC B 201
ChainResidue
BHIS24
BHIS24
BPHE70
BPHE70
BMET71
BMET71
BASN72
BASN118
BASN118
BASN14
BASN14

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

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PDB entries from 2024-05-29

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