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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6CX8

Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Vibrio cholerae in complex with manganese ions.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0006598biological_processpolyamine catabolic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0046203biological_processspermidine catabolic process
A0046208biological_processspermine catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004145molecular_functiondiamine N-acetyltransferase activity
B0005737cellular_componentcytoplasm
B0006598biological_processpolyamine catabolic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0046203biological_processspermidine catabolic process
B0046208biological_processspermine catabolic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004145molecular_functiondiamine N-acetyltransferase activity
C0005737cellular_componentcytoplasm
C0006598biological_processpolyamine catabolic process
C0016740molecular_functiontransferase activity
C0016746molecular_functionacyltransferase activity
C0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
C0046203biological_processspermidine catabolic process
C0046208biological_processspermine catabolic process
C0046872molecular_functionmetal ion binding
D0000287molecular_functionmagnesium ion binding
D0004145molecular_functiondiamine N-acetyltransferase activity
D0005737cellular_componentcytoplasm
D0006598biological_processpolyamine catabolic process
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
D0046203biological_processspermidine catabolic process
D0046208biological_processspermine catabolic process
D0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0004145molecular_functiondiamine N-acetyltransferase activity
E0005737cellular_componentcytoplasm
E0006598biological_processpolyamine catabolic process
E0016740molecular_functiontransferase activity
E0016746molecular_functionacyltransferase activity
E0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
E0046203biological_processspermidine catabolic process
E0046208biological_processspermine catabolic process
E0046872molecular_functionmetal ion binding
F0000287molecular_functionmagnesium ion binding
F0004145molecular_functiondiamine N-acetyltransferase activity
F0005737cellular_componentcytoplasm
F0006598biological_processpolyamine catabolic process
F0016740molecular_functiontransferase activity
F0016746molecular_functionacyltransferase activity
F0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
F0046203biological_processspermidine catabolic process
F0046208biological_processspermine catabolic process
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MN A 201
ChainResidue
AGLU33
AGLU75
BGLU33
BGLU75
site_idAC2
Number of Residues2
Detailsbinding site for residue IPA A 202
ChainResidue
AHIS122
AHOH322
site_idAC3
Number of Residues5
Detailsbinding site for residue PO4 A 203
ChainResidue
APHE98
AALA99
AGLY95
ALYS96
AGLY97
site_idAC4
Number of Residues1
Detailsbinding site for residue IPA B 201
ChainResidue
BILE27
site_idAC5
Number of Residues4
Detailsbinding site for residue MN C 201
ChainResidue
CGLU33
CGLU75
DGLU33
DGLU75
site_idAC6
Number of Residues1
Detailsbinding site for residue IPA C 202
ChainResidue
CGLU37
site_idAC7
Number of Residues5
Detailsbinding site for residue PO4 C 203
ChainResidue
CGLY95
CLYS96
CGLY97
CPHE98
CALA99
site_idAC8
Number of Residues7
Detailsbinding site for residue PO4 D 201
ChainResidue
DGLY95
DLYS96
DGLY97
DPHE98
DALA99
DHOH313
DHOH320
site_idAC9
Number of Residues5
Detailsbinding site for residue MN E 201
ChainResidue
EGLU33
EGLU75
EHOH301
FGLU33
FGLU75
site_idAD1
Number of Residues4
Detailsbinding site for residue PO4 E 202
ChainResidue
EGLY95
EGLY97
EPHE98
EALA99
site_idAD2
Number of Residues3
Detailsbinding site for residue MPD F 201
ChainResidue
FVAL123
FALA124
FASN127
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues785
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with polyamine.","authors":["Filippova E.V.","Minasov G.","Shuvalova L.","Kiryukhina O.","Kuhn M.L.","Anderson W.F."]}},{"source":"PDB","id":"4MJ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26410587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CNP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsSite: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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