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3K9U

Crystal structure of paia acetyltransferase (ta0374) from thermoplasma acidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004145molecular_functiondiamine N-acetyltransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0043939biological_processnegative regulation of sporulation
B0004145molecular_functiondiamine N-acetyltransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0043939biological_processnegative regulation of sporulation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 160
ChainResidue
ATRP40
ATYR45
AARG91

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 161
ChainResidue
AHIS100
AACO164
BHIS100
BACO162

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 162
ChainResidue
ASER33
BGLU35

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 163
ChainResidue
AGLN58
AARG129

site_idAC5
Number of Residues32
DetailsBINDING SITE FOR RESIDUE ACO A 164
ChainResidue
ASER23
ATRP26
ATHR27
AARG91
ALEU92
ATYR93
ALEU94
ATHR99
AHIS100
ALYS101
ALYS102
AILE103
AGLY104
ALYS105
ATYR126
AASN131
AVAL133
AGLY134
ASER136
APHE137
ATYR138
ALYS140
ANI161
AHOH174
AHOH176
AHOH177
AHOH178
AHOH179
AHOH182
AHOH188
BHIS100
BACO162

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 160
ChainResidue
BARG129
BHOH188

site_idAC7
Number of Residues33
DetailsBINDING SITE FOR RESIDUE ACO B 162
ChainResidue
AHIS100
ANI161
AACO164
AHOH182
BTRP26
BTHR27
BLEU89
BLEU90
BARG91
BLEU92
BTYR93
BLEU94
BTHR99
BHIS100
BLYS101
BLYS102
BILE103
BGLY104
BLYS105
BTYR126
BASN131
BVAL133
BGLY134
BSER136
BPHE137
BTYR138
BLYS140
BHOH167
BHOH168
BHOH169
BHOH170
BHOH171
BHOH172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951
ChainResidueDetails
ATYR138
BTYR138

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:21633970
ChainResidueDetails
ALEU92
BLYS140
ATHR99
AASN131
ASER136
ALYS140
BLEU92
BTHR99
BASN131
BSER136

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: May have an important role in the acetylation of the polyamine => ECO:0000250|UniProtKB:P21340
ChainResidueDetails
AGLY142
BGLY142

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PDB entries from 2024-11-06

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