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2BXS

Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form B

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005829cellular_componentcytosol
A0006576biological_processbiogenic amine metabolic process
A0006584biological_processcatecholamine metabolic process
A0008131molecular_functionprimary amine oxidase activity
A0009967biological_processpositive regulation of signal transduction
A0016491molecular_functionoxidoreductase activity
A0042420biological_processdopamine catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0052595molecular_functionaliphatic amine oxidase activity
A0097621molecular_functionmonoamine oxidase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005829cellular_componentcytosol
B0006576biological_processbiogenic amine metabolic process
B0006584biological_processcatecholamine metabolic process
B0008131molecular_functionprimary amine oxidase activity
B0009967biological_processpositive regulation of signal transduction
B0016491molecular_functionoxidoreductase activity
B0042420biological_processdopamine catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0052595molecular_functionaliphatic amine oxidase activity
B0097621molecular_functionmonoamine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
AILE19
AGLY50
AARG51
AGLY66
AGLY67
AALA68
ATYR69
AHIS242
APRO243
AVAL244
AILE273
AGLY20
ATRP397
ATYR402
ACYS406
ATYR407
AGLY434
ATHR435
AGLY443
ATYR444
AMET445
AMLG601
AGLY22
AILE23
ASER24
ALEU42
AGLU43
AALA44
AARG45

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLG A 601
ChainResidue
AGLU216
ACYS323
AILE335
ALEU337
APHE352
ATYR407
AFAD600

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD B 600
ChainResidue
BILE19
BGLY20
BGLY22
BSER24
BLEU42
BGLU43
BALA44
BGLY50
BARG51
BGLY67
BALA68
BTYR69
BHIS242
BPRO243
BVAL244
BILE273
BTRP397
BTYR402
BCYS406
BTYR407
BGLY434
BTHR435
BGLY443
BTYR444
BMET445
BMLG601

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLG B 601
ChainResidue
BGLU216
BCYS323
BILE335
BLEU337
BPHE352
BTYR407
BFAD600

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues992
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18391214
ChainResidueDetails
AMET1-SER497
BMET1-SER497

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical; Anchor for type IV membrane protein
ChainResidueDetails
AVAL498-LEU518
BVAL498-LEU518

site_idSWS_FT_FI3
Number of Residues16
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:18391214
ChainResidueDetails
ATYR519-SER527
BTYR519-SER527

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for substrate specificity => ECO:0000250
ChainResidueDetails
AILE335
BILE335

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity
ChainResidueDetails
ACYS374
BCYS374

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|PubMed:11812236
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21396
ChainResidueDetails
ASER383
BSER383

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: S-8alpha-FAD cysteine => ECO:0000269|PubMed:18391214, ECO:0007744|PDB:2BXR, ECO:0007744|PDB:2BXS, ECO:0007744|PDB:2Z5X, ECO:0007744|PDB:2Z5Y
ChainResidueDetails
ACYS406
BCYS406

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
AGLY71

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b5q
ChainResidueDetails
BGLY71

224572

PDB entries from 2024-09-04

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