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3CNS

Crystal structure of fms1 in complex with S-Bz-MeSpermidine

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 Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 517
ChainResidue
AILE14
AGLY45
AGLY46
AARG47
AGLY62
AALA63
ASER64
ATRP65
AHIS67
ACYS221
ATHR252
AGLY15
APRO254
AGLY270
ALEU294
ATRP440
ATYR445
AALA449
ATYR450
AGLY478
AGLU479
AGLY487
AGLY17
ACYS488
AALA489
AALA492
AILE18
AALA19
ALEU38
AGLU39
AALA40
AARG41

site_idAC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD B 517
ChainResidue
BGLY15
BGLY17
BILE18
BALA19
BLEU38
BGLU39
BALA40
BARG41
BGLY46
BARG47
BGLY62
BALA63
BSER64
BTRP65
BHIS67
BCYS221
BTHR252
BPRO254
BGLY270
BLEU294
BTRP440
BTYR445
BALA449
BTYR450
BGLY478
BGLU479
BGLY487
BCYS488
BALA489
BALA492

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SP8 A 518
ChainResidue
ATRP65
AHIS67
AASP94
ALEU173
ATRP174
ALEU294
ALYS312
ALEU375
ATYR450

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SP8 B 518
ChainResidue
BTRP65
BHIS67
BLEU173
BTRP174
BLEU294
BLEU375
BTYR450
BGLY487

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
AGLY193
ALYS296

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BGLY193
BLYS296

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
AHIS67

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f8r
ChainResidueDetails
BHIS67

222415

PDB entries from 2024-07-10

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