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4HOY

Crystal structure of Peptidyl- tRNA Hydrolase from Acinetobacter baumannii at 1.78 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 Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
APRO13
AGLY14
AGLU30
AMET66
AHOH322
AHOH360
AHOH487

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
APRO78
AHOH305
AHOH520
ALYS45
APHE46

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
AASP43
APRO44
AGLY48

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 204
ChainResidue
ALYS107
AGLY111
AHIS112
AARG131
AARG133
AHOH307
AHOH403

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 205
ChainResidue
ATYR36
AASN54
AGLU56
ATYR83
AGLN84
AHOH404
AHOH433

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 206
ChainResidue
AGLU16
ATYR17
ASER146
ALEU150
ALEU150
AHOH443
AHOH453
AHOH453

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PEG A 207
ChainResidue
ATYR36
AGLY37
AILE38
ATHR39
AARG52
AGLY53
AASN54
APRO127
AHOH346
AHOH510
AHOH514

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 208
ChainResidue
APRO13
AASN70
AARG71
AHOH343
AHOH399
AHOH435

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

222036

PDB entries from 2024-07-03

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