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

3ANX

Crystal structure of triamine/agmatine aminopropyltransferase (SPEE) from thermus thermophilus, complexed with MTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004766molecular_functionspermidine synthase activity
A0005737cellular_componentcytoplasm
A0006596biological_processpolyamine biosynthetic process
A0008295biological_processspermidine biosynthetic process
A0010487molecular_functionthermospermine synthase activity
A0016740molecular_functiontransferase activity
A0016768molecular_functionspermine synthase activity
A0043918molecular_functioncadaverine aminopropyltransferase activity
A0043919molecular_functionagmatine aminopropyltransferase activity
B0003824molecular_functioncatalytic activity
B0004766molecular_functionspermidine synthase activity
B0005737cellular_componentcytoplasm
B0006596biological_processpolyamine biosynthetic process
B0008295biological_processspermidine biosynthetic process
B0010487molecular_functionthermospermine synthase activity
B0016740molecular_functiontransferase activity
B0016768molecular_functionspermine synthase activity
B0043918molecular_functioncadaverine aminopropyltransferase activity
B0043919molecular_functionagmatine aminopropyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MTA A 315
ChainResidue
AGLN33
AALA141
AASP158
ATHR160
ALEU172
AGLN54
AGLY85
AGLY86
AGLY87
AASP108
AILE109
ALEU113
AASP140

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MTA B 315
ChainResidue
BGLN33
BGLY85
BGLY86
BGLY87
BVAL107
BASP108
BILE109
BLEU113
BALA141
BASP158
BLEU159
BLEU172

Functional Information from PROSITE/UniProt
site_idPS01330
Number of Residues14
DetailsPABS_1 Polyamine biosynthesis (PABS) domain signature. VLIVGGGeGatLrE
ChainResidueDetails
AVAL81-GLU94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00198
ChainResidueDetails
AASP158
BASP158

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:21458463, ECO:0007744|PDB:3ANX
ChainResidueDetails
AGLN33
AASP108
AASP140
BGLN33
BASP108
BASP140

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00198
ChainResidueDetails
AHIS64
AGLU88
AASP158
APRO168
BHIS64
BGLU88
BASP158
BPRO168

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon