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3BNU

Crystal structure of polyamine oxidase FMS1 from Saccharomyces cerevisiae in complex with bis-(3S,3'S)-methylated spermine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0015940biological_processpantothenate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046208biological_processspermine catabolic process
A0046592molecular_functionpolyamine oxidase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0052897molecular_functionN8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
A0052901molecular_functionspermine:oxygen oxidoreductase (spermidine-forming) activity
A0052902molecular_functionspermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity
A0052903molecular_functionN1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
A0052904molecular_functionN1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
B0003682molecular_functionchromatin binding
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
B0015940biological_processpantothenate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046208biological_processspermine catabolic process
B0046592molecular_functionpolyamine oxidase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0052897molecular_functionN8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
B0052901molecular_functionspermine:oxygen oxidoreductase (spermidine-forming) activity
B0052902molecular_functionspermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity
B0052903molecular_functionN1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
B0052904molecular_functionN1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD B 802
ChainResidue
BGLY15
BGLY62
BALA63
BSER64
BTRP65
BHIS67
BCYS221
BVAL223
BTHR252
BVAL253
BGLY270
BGLY17
BLEU294
BTYR445
BALA449
BTYR450
BGLY478
BGLU479
BGLY487
BCYS488
BALA489
BALA492
BILE18
BSPZ803
BHOH807
BHOH818
BHOH829
BHOH893
BHOH905
BHOH909
BHOH911
BALA19
BGLU39
BALA40
BARG41
BGLY46
BARG47

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SPZ B 803
ChainResidue
BTRP65
BHIS67
BLEU173
BTRP174
BPHE189
BLEU294
BTYR450
BALA486
BCYS488
BFAD802

site_idAC3
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 801
ChainResidue
AGLY15
AGLY17
AILE18
AALA19
AGLU39
AALA40
AARG41
AGLY46
AARG47
AGLY62
AALA63
ASER64
ATRP65
AHIS67
AVAL223
ATHR252
AVAL253
AGLY270
ALEU294
ATYR445
AALA449
ATYR450
AGLY478
AGLU479
AGLY487
ACYS488
AALA489
AALA492
ASPZ802
AHOH803
AHOH809
AHOH814
AHOH820
AHOH827
AHOH830
AHOH839

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SPZ A 802
ChainResidue
ATRP65
AHIS67
AASP68
ALEU173
ATRP174
APHE189
ALEU375
ATYR450
AALA486
ACYS488
AFAD801

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BGLY193
BLYS296

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
AGLY193
ALYS296

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BHIS67

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
AHIS67

222415

PDB entries from 2024-07-10

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