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5UG4

Structure of spermidine N-acetyltransferase SpeG from Vibrio cholerae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0006598biological_processpolyamine catabolic process
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
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
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 Residues5
Detailsbinding site for residue CA A 201
ChainResidue
AGLU33
AGLU75
AHOH362
CGLU75
CCA201

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 202
ChainResidue
BHOH329
BHOH361
AGLU34
APRO35
AGLU41
BASN53

site_idAC3
Number of Residues2
Detailsbinding site for residue ACT A 203
ChainResidue
AASN22
AHOH306

site_idAC4
Number of Residues4
Detailsbinding site for residue MRD A 204
ChainResidue
AHIS122
AVAL123
AALA124
AHOH376

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 201
ChainResidue
BGLU33
BGLU33
BGLU75
BGLU75
BHOH302
BHOH302

site_idAC6
Number of Residues5
Detailsbinding site for residue CA B 202
ChainResidue
BGLU33
BGLU75
BGLU75
BCA203
BHOH364

site_idAC7
Number of Residues4
Detailsbinding site for residue CA B 203
ChainResidue
BGLU33
BGLU75
BGLU75
BCA202

site_idAC8
Number of Residues6
Detailsbinding site for residue CA B 204
ChainResidue
BGLU34
BPRO35
BGLU41
CASN53
CHOH304
CHOH328

site_idAC9
Number of Residues1
Detailsbinding site for residue ACT B 205
ChainResidue
BILE151

site_idAD1
Number of Residues1
Detailsbinding site for residue EOH B 206
ChainResidue
BASN53

site_idAD2
Number of Residues8
Detailsbinding site for residue CA C 201
ChainResidue
AGLU33
AGLU75
ACA201
AHOH344
CGLU33
CGLU75
CCA202
CHOH306

site_idAD3
Number of Residues6
Detailsbinding site for residue CA C 202
ChainResidue
AGLU75
AHOH316
CGLU33
CGLU75
CCA201
CHOH346

site_idAD4
Number of Residues6
Detailsbinding site for residue CA C 203
ChainResidue
AASN53
AHOH317
AHOH364
CGLU34
CPRO35
CGLU41

site_idAD5
Number of Residues2
Detailsbinding site for residue ACT C 204
ChainResidue
CILE151
CHOH353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951
ChainResidueDetails
ATYR134
BTYR134
CTYR134

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|Ref.3, ECO:0007744|PDB:4MJ8
ChainResidueDetails
AMET28
AGLU84
BMET28
BGLU84
CMET28
CGLU84

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4
ChainResidueDetails
AGLU33
BGLU33
CGLU33

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4MI4, ECO:0007744|PDB:4R87
ChainResidueDetails
AGLU41
BGLU41
CGLU41

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R87
ChainResidueDetails
AHIS49
BHIS49
CHIS49

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0000269|PubMed:26410587, ECO:0007744|PDB:5CNP
ChainResidueDetails
AGLU75
BGLU75
CGLU75

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57, ECO:0007744|PDB:4R87
ChainResidueDetails
AILE87
AGLN94
BILE87
BGLN94
CILE87
CGLN94

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25623305, ECO:0007744|PDB:4R57
ChainResidueDetails
AASN127
BASN127
CASN127

site_idSWS_FT_FI9
Number of Residues3
DetailsSITE: Could be important for selectivity toward long polyamines => ECO:0000305|PubMed:25623305
ChainResidueDetails
AGLU84
BGLU84
CGLU84

225946

PDB entries from 2024-10-09

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