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2B3U

Human Spermine spermidine acetyltransferase K26R mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006596biological_processpolyamine biosynthetic 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
A0042802molecular_functionidentical protein binding
B0001525biological_processangiogenesis
B0004145molecular_functiondiamine N-acetyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006596biological_processpolyamine biosynthetic 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
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 172
ChainResidue
BARG142
BARG143

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 172
ChainResidue
AARG142
AARG143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951
ChainResidueDetails
ATYR140
BTYR140

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000305|PubMed:17516632
ChainResidueDetails
ATYR27
BGLU92
BPHE94
BGLY102
BHIS126
BASN133
BTYR140
BGLU152
AGLU92
APHE94
AGLY102
AHIS126
AASN133
ATYR140
AGLU152
BTYR27

218853

PDB entries from 2024-04-24

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