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3F0A

Structure of a putative n-acetyltransferase (ta0374) in complex with acetyl-coa from thermoplasma acidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004145molecular_functiondiamine N-acetyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0043939biological_processnegative regulation of sporulation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 160
ChainResidue
AHIS100
AACO162

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 161
ChainResidue
ATYR28
AHIS128
AASN131
AACO162

site_idAC3
Number of Residues33
DetailsBINDING SITE FOR RESIDUE ACO A 162
ChainResidue
AARG91
ALEU92
ATYR93
ALEU94
ATHR99
AHIS100
ALYS101
ALYS102
AILE103
AGLY104
ALYS105
ATYR126
AASN131
AVAL133
AGLY134
ASER136
APHE137
ATYR138
ALYS140
ANI160
ACL161
AHOH168
AHOH171
AHOH174
AHOH175
AHOH176
AHOH184
AHOH185
AHOH226
AHOH227
ATRP26
ATHR27
ALEU89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951
ChainResidueDetails
ATYR138

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:21633970
ChainResidueDetails
ALEU92
ATHR99
AASN131
ASER136
ALYS140

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: May have an important role in the acetylation of the polyamine => ECO:0000250|UniProtKB:P21340
ChainResidueDetails
AGLY142

237735

PDB entries from 2025-06-18

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