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4FOP

Crystal Structure of Peptidyl-tRNA hydrolase from Acinetobacter baumannii at 1.86 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
APRO13
AGLY14
AGLU30
AHOH322
AHOH361

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG A 202
ChainResidue
AARG52
AGLY53
AASN54
AHOH327
AHOH347
AHOH408
ATYR36
AGLY37
AILE38
ATHR39

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 203
ChainResidue
ALYS45
AHIS47
AGLN74
APRO78

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 204
ChainResidue
APRO44
AHIS47
AGLY48
AMET66
AARG71
AHOH369

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 205
ChainResidue
ALYS107
AGLY111
AHIS112
AARG131
AARG133
AHOH307
AHOH407

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 206
ChainResidue
ATYR36
AASN54
AGLU56
ATYR83
AGLN84
AHOH408
AHOH438

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 207
ChainResidue
AGLU16
ATYR17
ASER146
ALEU150
AHOH448
AHOH458
AHOH458

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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