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4MJ8

Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with polyamine

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE SPM A 201
ChainResidue
AASN22
AHOH329
BHIS49
BILE50
BASP52
BGLU55
BHOH361
AMET28
AGLU33
AGLU34
ATYR36
AGLU37
AGLU41
AHOH302
AHOH326

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SPM A 202
ChainResidue
ATYR30
ATRP31
AGLU33
AGLU84
APHE85
AGLN86
AILE87
ALEU121
AHIS122
AHOH381

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH A 203
ChainResidue
AHOH308
CSER172

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EOH A 204
ChainResidue
ALYS48

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SPM B 201
ChainResidue
BASN22
BMET28
BGLU33
BGLU34
BTYR36
BGLU41
BHOH301
BHOH351
BHOH404
CHIS49
CILE50
CASP52
CGLU55
CHOH302

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EOH B 202
ChainResidue
BLYS48

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE SPM C 201
ChainResidue
AHIS49
AILE50
AASP52
AGLU55
AHOH341
AHOH347
CASN22
CMET28
CGLU33
CGLU34
CTYR36
CGLU37
CGLU41
CHOH303
CHOH394

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH C 202
ChainResidue
CTRP31
CGLN86

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues471
DetailsDomain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
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 Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
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 Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
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 Residues24
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 Residues27
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsSite: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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