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1OJC

HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH N-(2-aminoethyl)-p-chlorobenzamide

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 PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A1502
ChainResidue
AGLY11
AGLY41
AARG42
ATHR43
AGLY57
AGLY58
ASER59
ATYR60
APRO234
AVAL235
AALA263
AGLY13
AILE264
ATRP388
ATYR393
ACYS397
ATYR398
AGLY425
ATHR426
AGLY434
ATYR435
AMET436
AILE14
ALAZ1503
AHOH2010
AHOH2023
AHOH2182
AHOH2183
AHOH2184
AHOH2185
AHOH2186
ASER15
ALEU33
AGLU34
AALA35
AARG36
AGLY40

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LAZ A1503
ChainResidue
ATYR60
ALEU171
ACYS172
AILE198
AILE199
AGLN206
APHE343
ATYR398
ATYR435
AFAD1502
AHOH2102
AHOH2187

site_idAC3
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD B1497
ChainResidue
BVAL10
BGLY11
BGLY13
BILE14
BSER15
BLEU33
BGLU34
BALA35
BARG36
BGLY40
BGLY41
BARG42
BTHR43
BGLY57
BGLY58
BSER59
BTYR60
BPRO234
BVAL235
BALA263
BILE264
BTRP388
BTYR393
BCYS397
BTYR398
BGLY425
BTHR426
BGLY434
BTYR435
BMET436
BLAZ1498
BHOH2018
BHOH2125
BHOH2183
BHOH2224
BHOH2225
BHOH2226
BHOH2227
BHOH2229

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE LAZ B1498
ChainResidue
BHOH2229
BTYR60
BLEU171
BCYS172
BILE198
BILE199
BGLN206
BPHE343
BTYR398
BTYR435
BFAD1497
BHOH2228

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

219140

PDB entries from 2024-05-01

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