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

7ZW3

Crystal Structure of human MAO B in complex with (Z)-N-benzyl-1-(8-hydroxyquinolin-2-yl)methanimine oxide (inhibitor 19)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0005515molecular_functionprotein binding
AAA0005739cellular_componentmitochondrion
AAA0005740cellular_componentmitochondrial envelope
AAA0005741cellular_componentmitochondrial outer membrane
AAA0008131molecular_functionprimary amine oxidase activity
AAA0009055molecular_functionelectron transfer activity
AAA0009410biological_processresponse to xenobiotic stimulus
AAA0009636biological_processresponse to toxic substance
AAA0010044biological_processresponse to aluminum ion
AAA0010269biological_processresponse to selenium ion
AAA0014063biological_processnegative regulation of serotonin secretion
AAA0016491molecular_functionoxidoreductase activity
AAA0019607biological_processphenylethylamine catabolic process
AAA0021762biological_processsubstantia nigra development
AAA0030425cellular_componentdendrite
AAA0032496biological_processresponse to lipopolysaccharide
AAA0042420biological_processdopamine catabolic process
AAA0042802molecular_functionidentical protein binding
AAA0043025cellular_componentneuronal cell body
AAA0045471biological_processresponse to ethanol
AAA0045964biological_processpositive regulation of dopamine metabolic process
AAA0048545biological_processresponse to steroid hormone
AAA0050660molecular_functionflavin adenine dinucleotide binding
AAA0050665biological_processhydrogen peroxide biosynthetic process
AAA0051412biological_processresponse to corticosterone
AAA0052595molecular_functionaliphatic amine oxidase activity
AAA0097621molecular_functionmonoamine oxidase activity
BBB0005515molecular_functionprotein binding
BBB0005739cellular_componentmitochondrion
BBB0005740cellular_componentmitochondrial envelope
BBB0005741cellular_componentmitochondrial outer membrane
BBB0008131molecular_functionprimary amine oxidase activity
BBB0009055molecular_functionelectron transfer activity
BBB0009410biological_processresponse to xenobiotic stimulus
BBB0009636biological_processresponse to toxic substance
BBB0010044biological_processresponse to aluminum ion
BBB0010269biological_processresponse to selenium ion
BBB0014063biological_processnegative regulation of serotonin secretion
BBB0016491molecular_functionoxidoreductase activity
BBB0019607biological_processphenylethylamine catabolic process
BBB0021762biological_processsubstantia nigra development
BBB0030425cellular_componentdendrite
BBB0032496biological_processresponse to lipopolysaccharide
BBB0042420biological_processdopamine catabolic process
BBB0042802molecular_functionidentical protein binding
BBB0043025cellular_componentneuronal cell body
BBB0045471biological_processresponse to ethanol
BBB0045964biological_processpositive regulation of dopamine metabolic process
BBB0048545biological_processresponse to steroid hormone
BBB0050660molecular_functionflavin adenine dinucleotide binding
BBB0050665biological_processhydrogen peroxide biosynthetic process
BBB0051412biological_processresponse to corticosterone
BBB0052595molecular_functionaliphatic amine oxidase activity
BBB0097621molecular_functionmonoamine oxidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues974
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AAASER2-VAL489
BBBSER2-VAL489

site_idSWS_FT_FI2
Number of Residues52
DetailsTRANSMEM: Helical; Anchor for type IV membrane protein
ChainResidueDetails
AAAPRO490-LEU516
BBBPRO490-LEU516

site_idSWS_FT_FI3
Number of Residues6
DetailsTOPO_DOM: Mitochondrial intermembrane
ChainResidueDetails
AAALEU517-VAL520
BBBLEU517-VAL520

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Important for catalytic activity
ChainResidueDetails
AAACYS156
AAACYS365
AAAHIS382
BBBCYS156
BBBCYS365
BBBHIS382

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:11049757
ChainResidueDetails
AAASER2
BBBSER2

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BW75
ChainResidueDetails
AAALYS52
BBBLYS52

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
AAACYS397
BBBCYS397

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon