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3KK0

Crystal structure of partially folded intermediate state of peptidyl-tRNA hydrolase from Mycobacterium smegmatis

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 Residues1
DetailsBINDING SITE FOR RESIDUE IPA A 192
ChainResidue
AARG143

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IPA A 193
ChainResidue
AGLU152
AHOH257

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IPA A 194
ChainResidue
AILE177
AHOH360
AEDO6076

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 6073
ChainResidue
AASP95
ALEU97
AHIS115

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 6074
ChainResidue
AGLY53
AHOH318
AHOH343
AEDO6075

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 6075
ChainResidue
AEDO6074

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 6076
ChainResidue
ALYS44
ALYS45
AIPA194

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 6070
ChainResidue
APRO13
ASER68

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A 2053
ChainResidue
ALYS107
AGLY111
AARG132
AARG134

Functional Information from PROSITE/UniProt
site_idPS01195
Number of Residues14
DetailsPEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. YakTRHNlGfmVAD
ChainResidueDetails
ATYR17-ASP30

site_idPS01196
Number of Residues11
DetailsPEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. GeggHNGLRSV
ChainResidueDetails
AGLY111-VAL121

226262

PDB entries from 2024-10-16

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