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3BI5

Crystal structures of fms1 in complex with its inhibitors

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 801
ChainResidue
AILE14
AARG47
AGLY62
AALA63
ASER64
ATRP65
AHIS67
AVAL223
ATHR252
AVAL253
AGLY270
AGLY15
AALA449
ATYR450
AGLY478
AGLU479
AGLY487
ACYS488
AALA489
AALA492
ADIA2841
AHOH2842
AGLY17
AHOH2848
AHOH2852
AHOH2855
AILE18
AALA19
AGLU39
AALA40
AARG41
AGLY46

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DIA A 2841
ChainResidue
AHIS67
APHE97
ALEU173
ATRP174
APHE359
ATYR450
AFAD801

site_idAC3
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD B 802
ChainResidue
BGLY15
BILE18
BALA19
BGLU39
BALA40
BARG41
BGLY46
BARG47
BGLY62
BALA63
BSER64
BTRP65
BHIS67
BVAL223
BTHR252
BVAL253
BGLY270
BALA449
BTYR450
BGLY478
BGLU479
BGLY487
BCYS488
BALA489
BALA492
BDIA2842
BHOH2847

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DIA B 2842
ChainResidue
BHIS67
BLEU173
BTRP174
BPHE359
BTYR450
BGLY487
BCYS488
BFAD802

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

223790

PDB entries from 2024-08-14

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