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

6O64

Crystal Structure of Arabidopsis thaliana Spermidine Synthase isoform 2 (AtSPDS2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006595biological_processpolyamine metabolic process
B0003824molecular_functioncatalytic activity
B0006595biological_processpolyamine metabolic process
C0003824molecular_functioncatalytic activity
C0006595biological_processpolyamine metabolic process
D0003824molecular_functioncatalytic activity
D0006595biological_processpolyamine metabolic process
E0003824molecular_functioncatalytic activity
E0006595biological_processpolyamine metabolic process
F0003824molecular_functioncatalytic activity
F0006595biological_processpolyamine metabolic process
G0003824molecular_functioncatalytic activity
G0006595biological_processpolyamine metabolic process
H0003824molecular_functioncatalytic activity
H0006595biological_processpolyamine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue ACT A 401
ChainResidue
BSER270

site_idAC2
Number of Residues7
Detailsbinding site for residue PEG A 402
ChainResidue
AGLN101
AASP205
ASER206
AASP208
ATYR274
APRO275
AHOH519

site_idAC3
Number of Residues9
Detailsbinding site for residue PEG B 401
ChainResidue
BTYR110
BASP205
BSER206
BASP208
BTYR274
BPRO275
BHOH508
BHOH535
BGLN101

site_idAC4
Number of Residues1
Detailsbinding site for residue FMT B 402
ChainResidue
BSER306

site_idAC5
Number of Residues8
Detailsbinding site for residue PEG C 401
ChainResidue
CGLN101
CTYR110
CASP205
CSER206
CASP208
CGLN238
CTYR274
CHOH542

site_idAC6
Number of Residues5
Detailsbinding site for residue MLI D 401
ChainResidue
CVAL278
CHOH507
DSER270
DHOH520
DHOH545

site_idAC7
Number of Residues7
Detailsbinding site for residue PEG D 402
ChainResidue
DGLN101
DTYR110
DASP205
DSER206
DASP208
DGLN238
DTYR274

site_idAC8
Number of Residues2
Detailsbinding site for residue PEG D 403
ChainResidue
DTRP51
DHOH544

site_idAC9
Number of Residues2
Detailsbinding site for residue PEG D 404
ChainResidue
DPRO49
DTRP51

site_idAD1
Number of Residues3
Detailsbinding site for residue MLI E 401
ChainResidue
EHOH548
FALA323
FHOH536

site_idAD2
Number of Residues10
Detailsbinding site for residue EDO E 402
ChainResidue
EGLN111
EGLY133
EGLY134
EASP135
EGLY136
EGLY137
EVAL138
ELEU139
EHOH504
EHOH597

site_idAD3
Number of Residues5
Detailsbinding site for residue MLI E 403
ChainResidue
EGLU155
EILE156
EGLY185
EASP186
EGLY187

site_idAD4
Number of Residues11
Detailsbinding site for residue PEG E 404
ChainResidue
EVAL99
EGLN101
ETYR110
EASP205
ESER206
EASP208
ETYR274
EPRO275
EHOH502
EHOH520
EHOH538

site_idAD5
Number of Residues3
Detailsbinding site for residue FMT E 405
ChainResidue
EPHE330
FHOH585
FHOH591

site_idAD6
Number of Residues6
Detailsbinding site for residue FMT E 406
ChainResidue
EASN265
ETYR266
ELYS294
EPHE325
EHOH625
GGLN290

site_idAD7
Number of Residues4
Detailsbinding site for residue ACT F 401
ChainResidue
EALA323
FSER322
FALA323
FHOH551

site_idAD8
Number of Residues8
Detailsbinding site for residue PEG F 402
ChainResidue
FTYR110
FASP205
FSER206
FASP208
FGLN238
FTYR274
FPRO275
FHOH537

site_idAD9
Number of Residues8
Detailsbinding site for residue PEG F 403
ChainResidue
HHOH513
FLYS126
FGLU149
FHOH504
FHOH622
HASN124
HLYS126
HSER147

site_idAE1
Number of Residues10
Detailsbinding site for residue PEG G 401
ChainResidue
GVAL99
GGLN101
GTYR110
GASP205
GSER206
GASP208
GTYR274
GHOH509
GHOH515
GHOH544

site_idAE2
Number of Residues4
Detailsbinding site for residue MLI H 401
ChainResidue
HTRP268
HSER270
HHOH501
HHOH535

site_idAE3
Number of Residues3
Detailsbinding site for residue ACT H 402
ChainResidue
GARG105
HTRP243
HHIS245

site_idAE4
Number of Residues3
Detailsbinding site for residue ACT H 403
ChainResidue
EHOH577
HSER322
HHOH586

site_idAE5
Number of Residues1
Detailsbinding site for residue ACT H 404
ChainResidue
HGLY50

Functional Information from PROSITE/UniProt
site_idPS01330
Number of Residues14
DetailsPABS_1 Polyamine biosynthesis (PABS) domain signature. VLVIGGGdGgvLrE
ChainResidueDetails
AVAL128-GLU141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP205
BASP205
CASP205
DASP205
EASP205
FASP205
GASP205
HASP205

site_idSWS_FT_FI2
Number of Residues64
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLN80
BTYR110
BGLN111
BASP135
BGLU155
BASP186
BASP205
BTYR274
CGLN80
CTYR110
CGLN111
ATYR110
CASP135
CGLU155
CASP186
CASP205
CTYR274
DGLN80
DTYR110
DGLN111
DASP135
DGLU155
AGLN111
DASP186
DASP205
DTYR274
EGLN80
ETYR110
EGLN111
EASP135
EGLU155
EASP186
EASP205
AASP135
ETYR274
FGLN80
FTYR110
FGLN111
FASP135
FGLU155
FASP186
FASP205
FTYR274
GGLN80
AGLU155
GTYR110
GGLN111
GASP135
GGLU155
GASP186
GASP205
GTYR274
HGLN80
HTYR110
HGLN111
AASP186
HASP135
HGLU155
HASP186
HASP205
HTYR274
AASP205
ATYR274
BGLN80

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon