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6QMM

Crystal structure of Synecochoccus Spermidine Synthase in complex with putrescine, spermidine and MTA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004766molecular_functionspermidine synthase activity
A0005737cellular_componentcytoplasm
A0006596biological_processpolyamine biosynthetic process
A0008295biological_processspermidine biosynthetic process
A0016740molecular_functiontransferase activity
B0003824molecular_functioncatalytic activity
B0004766molecular_functionspermidine synthase activity
B0005737cellular_componentcytoplasm
B0006596biological_processpolyamine biosynthetic process
B0008295biological_processspermidine biosynthetic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue PUT A 301
ChainResidue
AMET55
AGLY160
ASER161
AGLN192
ATYR227
ATRP232
AHOH417

site_idAC2
Number of Residues12
Detailsbinding site for residue SPD B 301
ChainResidue
BHIS65
BASP89
BASP159
BGLY160
BSER161
BASP162
BTYR227
BTRP232
BMTA302
BHOH401
BMET55
BTYR64

site_idAC3
Number of Residues19
Detailsbinding site for residue MTA B 302
ChainResidue
BGLN34
BLEU48
BLEU50
BMET55
BGLY86
BGLY88
BASP89
BVAL108
BGLU109
BILE110
BVAL114
BASP140
BGLY141
BILE142
BASP159
BGLY160
BPRO166
BALA167
BSPD301

site_idAC4
Number of Residues8
Detailsbinding site for residue PXN B 303
ChainResidue
BPRO185
BGLY186
BASP239
BTHR240
BGLN243
BHOH434
BHOH449
BHOH474

Functional Information from PROSITE/UniProt
site_idPS01330
Number of Residues14
DetailsPABS_1 Polyamine biosynthesis (PABS) domain signature. VLVIGGGdGgtVrE
ChainResidueDetails
BVAL82-GLU95
AVAL82-GLU95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00198
ChainResidueDetails
BASP159

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00198, ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM
ChainResidueDetails
BGLN34
BHIS65
BASP89
BGLU109
BASP140
BPRO166

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30877192, ECO:0007744|PDB:6QMM
ChainResidueDetails
BASP159

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PDB entries from 2024-07-10

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