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2C75

Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005740cellular_componentmitochondrial envelope
A0005741cellular_componentmitochondrial outer membrane
A0008131molecular_functionprimary methylamine oxidase activity
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0021762biological_processsubstantia nigra development
A0042420biological_processdopamine catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0050665biological_processhydrogen peroxide biosynthetic process
A0097621molecular_functionmonoamine oxidase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005740cellular_componentmitochondrial envelope
B0005741cellular_componentmitochondrial outer membrane
B0008131molecular_functionprimary methylamine oxidase activity
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0021762biological_processsubstantia nigra development
B0042420biological_processdopamine catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0050665biological_processhydrogen peroxide biosynthetic process
B0097621molecular_functionmonoamine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
AGLY11
AGLY41
AARG42
ATHR43
AGLY58
ASER59
ATYR60
AARG233
APRO234
AVAL235
AALA263
AGLY13
AILE264
ATRP388
ATYR393
ACYS397
ATYR398
AGLY425
ATHR426
AGLY434
ALEU435
AMET436
AILE14
AALA439
ARSA601
AHOH2029
AHOH2257
AHOH2405
AHOH2406
AHOH2407
AHOH2408
AHOH2409
AHOH2410
ASER15
ALEU33
AGLU34
AALA35
AARG36
AGLY40

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RSA A 601
ChainResidue
ALEU171
ACYS172
AILE198
AGLN206
ATYR326
APHE343
ATYR398
AFAD600

site_idAC3
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD B 600
ChainResidue
BGLY11
BGLY13
BILE14
BSER15
BLEU33
BGLU34
BALA35
BARG36
BGLY40
BGLY41
BARG42
BTHR43
BGLY58
BSER59
BTYR60
BARG233
BPRO234
BVAL235
BALA263
BILE264
BTRP388
BTYR393
BCYS397
BTYR398
BGLY425
BTHR426
BGLY434
BLEU435
BMET436
BALA439
BRSA601
BHOH2041
BHOH2304
BHOH2394
BHOH2467
BHOH2468
BHOH2469
BHOH2470
BHOH2471

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE RSA B 601
ChainResidue
BLEU171
BCYS172
BILE198
BGLN206
BTYR326
BPHE343
BTYR398
BFAD600

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues974
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AASN3-PRO490
BASN3-PRO490

site_idSWS_FT_FI2
Number of Residues52
DetailsTRANSMEM: Helical; Anchor for type IV membrane protein
ChainResidueDetails
AGLY491-LEU517
BGLY491-LEU517

site_idSWS_FT_FI3
Number of Residues6
DetailsTOPO_DOM: Mitochondrial intermembrane
ChainResidueDetails
ALEU517-VAL520
BLEU517-VAL520

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Important for catalytic activity
ChainResidueDetails
ATRP157
AGLU366
ATYR383
BTRP157
BGLU366
BTYR383

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757
ChainResidueDetails
AASN3
BASN3

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75
ChainResidueDetails
ATYR53
BTYR53

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-8alpha-FAD cysteine => ECO:0000269|PubMed:11753429, ECO:0000269|PubMed:12913124, ECO:0000269|PubMed:15027868, ECO:0000269|PubMed:15710600, ECO:0000269|PubMed:16366596, ECO:0007744|PDB:1GOS, ECO:0007744|PDB:1OJ9, ECO:0007744|PDB:1OJA, ECO:0007744|PDB:1OJC, ECO:0007744|PDB:1OJD, ECO:0007744|PDB:1S2Q, ECO:0007744|PDB:1S2Y, ECO:0007744|PDB:1S3B, ECO:0007744|PDB:1S3E, ECO:0007744|PDB:2BK3, ECO:0007744|PDB:2BK4, ECO:0007744|PDB:2BK5, ECO:0007744|PDB:2BYB, ECO:0007744|PDB:2C64, ECO:0007744|PDB:2C65, ECO:0007744|PDB:2C66, ECO:0007744|PDB:2C67, ECO:0007744|PDB:2C70, ECO:0007744|PDB:2C72, ECO:0007744|PDB:2C73, ECO:0007744|PDB:2C75, ECO:0007744|PDB:2C76, ECO:0007744|PDB:2V5Z, ECO:0007744|PDB:2V60, ECO:0007744|PDB:2V61, ECO:0007744|PDB:2VRL, ECO:0007744|PDB:2VRM, ECO:0007744|PDB:2VZ2, ECO:0007744|PDB:2XFN, ECO:0007744|PDB:2XFO, ECO:0007744|PDB:2XFP, ECO:0007744|PDB:2XFQ, ECO:0007744|PDB:3PO7, ECO:0007744|PDB:3ZYX, ECO:0007744|PDB:4A79, ECO:0007744|PDB:4A7A, ECO:0007744|PDB:4CRT, ECO:0007744|PDB:5MRL
ChainResidueDetails
ATYR398
BTYR398

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
AGLY62

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
BGLY62

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PDB entries from 2025-06-11

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