Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6CY6

Crystal structure of spermidine/spermine N-acetyltransferase SpeG from Escherichia coli in complex with tris(hydroxymethyl)aminomethane.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005737cellular_componentcytoplasm
A0006598biological_processpolyamine catabolic process
A0015936biological_processcoenzyme A metabolic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046203biological_processspermidine catabolic process
A0046208biological_processspermine catabolic process
A0046872molecular_functionmetal ion binding
A1990235cellular_componentdiamine N-acetyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 201
ChainResidue
AGLU15
AARG18
AHOH332
AHOH404

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 202
ChainResidue
AMET30
AARG31
ATYR32
AARG59
AHOH333

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 203
ChainResidue
AASP125
AASN128

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 204
ChainResidue
AARG31
AMPD212

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 205
ChainResidue
AARG14
ASER45

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 206
ChainResidue
ALYS126
AARG136
AVAL142

site_idAC7
Number of Residues1
Detailsbinding site for residue CL A 207
ChainResidue
ATYR156

site_idAC8
Number of Residues2
Detailsbinding site for residue CL A 208
ChainResidue
AARG14
AHOH404

site_idAC9
Number of Residues6
Detailsbinding site for residue NA A 209
ChainResidue
AGLU36
AASP54
AGLU57
AARG58
AHOH321
AHOH365

site_idAD1
Number of Residues7
Detailsbinding site for residue TRS A 210
ChainResidue
ATYR32
ATRP33
AASP54
ASER56
AGLU57
AGLU76
AHOH302

site_idAD2
Number of Residues6
Detailsbinding site for residue MRD A 211
ChainResidue
ALEU12
AHIS51
AGLU57
AARG58
AARG59
AHOH321

site_idAD3
Number of Residues1
Detailsbinding site for residue MPD A 212
ChainResidue
ACL204

site_idAD4
Number of Residues1
Detailsbinding site for residue MRD A 213
ChainResidue
AASN128

site_idAD5
Number of Residues4
Detailsbinding site for residue MPD A 214
ChainResidue
ATYR32
AILE123
ALEU146
AGLU149

site_idAD6
Number of Residues4
Detailsbinding site for residue MPD A 215
ChainResidue
ALYS126
AGLU143
AGLU145
AILE160

site_idAD7
Number of Residues4
Detailsbinding site for residue MPD A 216
ChainResidue
AILE123
AASP125
APHE150
AILE152

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:33826189
ChainResidueDetails
ATYR135

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9KL03
ChainResidueDetails
AMET30
AGLU35
AGLU43
AHIS51
AGLU85
AILE88
AGLN95
AASN128

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31205017, ECO:0007744|PDB:4R9M
ChainResidueDetails
AGLU76

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Could be important for selectivity toward long polyamines => ECO:0000250|UniProtKB:Q9KL03
ChainResidueDetails
AGLU85

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon