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4FOT

Crystal structure of Peptidyl- tRNA Hydrolase from Acinetobacter baumannii at 2.20 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 Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
AGLY14
AGLU30
AMET66
AHOH377
AHOH390

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
AGLY111
AHIS112
AVAL122
APRO123
AHOH419
AASP34
AGLY37
AILE38
ATHR39

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 203
ChainResidue
AGLY73
AGLN74
AASP120
AHOH355

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 2024-07-10

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