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

7B0V

Crystal Structure of human monoamine oxidase B in complex with (E)-3-phenyl-1-(3-(trifluoromethyl)phenyl)prop-2-en-1-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005740cellular_componentmitochondrial envelope
A0005741cellular_componentmitochondrial outer membrane
A0008131molecular_functionprimary amine oxidase activity
A0009055molecular_functionelectron transfer activity
A0009410biological_processresponse to xenobiotic stimulus
A0009636biological_processresponse to toxic substance
A0010044biological_processresponse to aluminum ion
A0010269biological_processresponse to selenium ion
A0014063biological_processnegative regulation of serotonin secretion
A0016491molecular_functionoxidoreductase activity
A0019607biological_processphenylethylamine catabolic process
A0021762biological_processsubstantia nigra development
A0030425cellular_componentdendrite
A0032496biological_processresponse to lipopolysaccharide
A0042420biological_processdopamine catabolic process
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0045471biological_processresponse to ethanol
A0045964biological_processpositive regulation of dopamine metabolic process
A0048545biological_processresponse to steroid hormone
A0050660molecular_functionflavin adenine dinucleotide binding
A0050665biological_processhydrogen peroxide biosynthetic process
A0051412biological_processresponse to corticosterone
A0052595molecular_functionaliphatic amine oxidase activity
A0097621molecular_functionmonoamine oxidase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005740cellular_componentmitochondrial envelope
B0005741cellular_componentmitochondrial outer membrane
B0008131molecular_functionprimary amine oxidase activity
B0009055molecular_functionelectron transfer activity
B0009410biological_processresponse to xenobiotic stimulus
B0009636biological_processresponse to toxic substance
B0010044biological_processresponse to aluminum ion
B0010269biological_processresponse to selenium ion
B0014063biological_processnegative regulation of serotonin secretion
B0016491molecular_functionoxidoreductase activity
B0019607biological_processphenylethylamine catabolic process
B0021762biological_processsubstantia nigra development
B0030425cellular_componentdendrite
B0032496biological_processresponse to lipopolysaccharide
B0042420biological_processdopamine catabolic process
B0042802molecular_functionidentical protein binding
B0043025cellular_componentneuronal cell body
B0045471biological_processresponse to ethanol
B0045964biological_processpositive regulation of dopamine metabolic process
B0048545biological_processresponse to steroid hormone
B0050660molecular_functionflavin adenine dinucleotide binding
B0050665biological_processhydrogen peroxide biosynthetic process
B0051412biological_processresponse to corticosterone
B0052595molecular_functionaliphatic amine oxidase activity
B0097621molecular_functionmonoamine oxidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues974
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
BSER2-VAL489
ASER2-VAL489

site_idSWS_FT_FI2
Number of Residues52
DetailsTRANSMEM: Helical; Anchor for type IV membrane protein
ChainResidueDetails
APRO490-LEU516
BPRO490-LEU516

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
BCYS156
BCYS365
BHIS382
ACYS156
ACYS365
AHIS382

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757
ChainResidueDetails
BSER2
ASER2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75
ChainResidueDetails
BLYS52
ALYS52

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
BCYS397
ACYS397

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon