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2FXF

Human spermidine/spermine N1-acetyltransferase

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
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
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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU92
AASP93
AHOH1001
AHOH1002
AHOH1003
AHOH1004

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 302
ChainResidue
BHOH2022
BHOH2078
BHOH2081
BGLU92
BASP93
BHOH2007

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
ACYS120

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 304
ChainResidue
BARG119
BCYS120

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 305
ChainResidue
AALA12
ASER15
AHOH1082
AHOH1111

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 801
ChainResidue
AGLU28
AVAL129
AALA130
AASN133
AACO1000

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ACO A 1000
ChainResidue
ATYR27
AGLU92
APHE94
APHE95
AVAL96
AARG101
AGLY102
APHE103
AGLY104
AILE105
AGLY106
ASER107
AASN133
ASER136
APHE139
ATYR140
AARG142
AARG143
AACT801
AHOH1010
AHOH1068
AHOH1128

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ACO B 2000
ChainResidue
BTYR27
BGLU92
BPHE94
BPHE95
BVAL96
BARG101
BARG101
BGLY102
BPHE103
BGLY104
BILE105
BGLY106
BSER107
BLEU128
BASN133
BPRO135
BSER136
BTYR140
BARG142
BARG143
BHOH2009
BHOH2050
BHOH2050
BHOH2068

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

219140

PDB entries from 2024-05-01

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