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3BJ7

Spermine/spermidine N1-acetyltransferase from mouse: Crystal structure of a ternary complex reveals solvent-mediated spermine binding

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005829cellular_componentcytosol
A0006595biological_processpolyamine metabolic process
A0006596biological_processpolyamine biosynthetic process
A0006598biological_processpolyamine catabolic process
A0008080molecular_functionN-acetyltransferase activity
A0009447biological_processputrescine catabolic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019809molecular_functionspermidine binding
A0032918biological_processspermidine acetylation
A0042127biological_processregulation of cell population proliferation
A0042802molecular_functionidentical protein binding
A0046208biological_processspermine catabolic process
B0001525biological_processangiogenesis
B0004145molecular_functiondiamine N-acetyltransferase activity
B0005829cellular_componentcytosol
B0006595biological_processpolyamine metabolic process
B0006596biological_processpolyamine biosynthetic process
B0006598biological_processpolyamine catabolic process
B0008080molecular_functionN-acetyltransferase activity
B0009447biological_processputrescine catabolic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0019809molecular_functionspermidine binding
B0032918biological_processspermidine acetylation
B0042127biological_processregulation of cell population proliferation
B0042802molecular_functionidentical protein binding
B0046208biological_processspermine catabolic process
C0001525biological_processangiogenesis
C0004145molecular_functiondiamine N-acetyltransferase activity
C0005829cellular_componentcytosol
C0006595biological_processpolyamine metabolic process
C0006596biological_processpolyamine biosynthetic process
C0006598biological_processpolyamine catabolic process
C0008080molecular_functionN-acetyltransferase activity
C0009447biological_processputrescine catabolic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0019809molecular_functionspermidine binding
C0032918biological_processspermidine acetylation
C0042127biological_processregulation of cell population proliferation
C0042802molecular_functionidentical protein binding
C0046208biological_processspermine catabolic process
D0001525biological_processangiogenesis
D0004145molecular_functiondiamine N-acetyltransferase activity
D0005829cellular_componentcytosol
D0006595biological_processpolyamine metabolic process
D0006596biological_processpolyamine biosynthetic process
D0006598biological_processpolyamine catabolic process
D0008080molecular_functionN-acetyltransferase activity
D0009447biological_processputrescine catabolic process
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0019809molecular_functionspermidine binding
D0032918biological_processspermidine acetylation
D0042127biological_processregulation of cell population proliferation
D0042802molecular_functionidentical protein binding
D0046208biological_processspermine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE COA A 400
ChainResidue
AGLU92
ASER107
APHE139
AARG142
AARG143
APHE94
APHE95
AARG101
AGLY102
APHE103
AGLY104
AILE105
AGLY106

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE COA B 401
ChainResidue
BGLU92
BPHE94
BPHE95
BARG101
BGLY102
BPHE103
BGLY104
BILE105
BGLY106
BSER107
BASN133
BSER136
BPHE139
BTYR140
BARG142
BARG143
CGLU134
CASN138

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE COA C 402
ChainResidue
CPHE94
CPHE95
CARG101
CGLY102
CPHE103
CGLY104
CGLY106
CSER107
CASN133
CSER136
CTYR140
CARG142
CARG143

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE COA D 403
ChainResidue
ATYR27
ATYR29
ASER98
ATRP132
DGLU92
DPHE94
DPHE95
DARG101
DGLY102
DPHE103
DGLY104
DILE105
DGLY106
DSER107
DASN133
DSER136
DPHE139
DTYR140
DARG142
DARG143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P21673","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues64
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18690703","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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