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

3BNM

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0003682molecular_functionchromatin binding
A0005737cellular_componentcytoplasm
A0015940biological_processpantothenate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
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
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0003682molecular_functionchromatin binding
B0005737cellular_componentcytoplasm
B0015940biological_processpantothenate biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0045944biological_processpositive regulation of transcription by RNA polymerase II
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 Residues33
DetailsBINDING SITE FOR RESIDUE FAD B 802
ChainResidue
BGLY15
BARG47
BGLY62
BALA63
BSER64
BTRP65
BHIS67
BCYS221
BVAL223
BTHR252
BVAL253
BGLY17
BGLY270
BLEU294
BALA449
BTYR450
BGLY478
BGLU479
BGLY487
BCYS488
BALA489
BALA492
BILE18
BSPJ803
BHOH805
BHOH809
BHOH886
BALA19
BLEU38
BGLU39
BALA40
BARG41
BGLY46

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SPJ B 803
ChainResidue
BTRP65
BHIS67
BASP68
BTRP174
BGLY190
BTYR450
BGLY485
BALA486
BCYS488
BTYR490
BFAD802

site_idAC3
Number of Residues35
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
ASPJ802
AHOH803
AHOH805
AHOH808
AHOH830
AHOH839
AHOH849

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SPJ A 802
ChainResidue
ATRP65
AHIS67
ALEU173
ATRP174
AASN195
ALEU375
ATYR450
AALA486
AGLY487
ACYS488
AFAD801

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon