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2Z5X

Crystal Structure of Human Monoamine Oxidase A with Harmine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0006576biological_processbiogenic amine metabolic process
A0006584biological_processcatecholamine metabolic process
A0008131molecular_functionprimary methylamine oxidase activity
A0016491molecular_functionoxidoreductase activity
A0019607biological_processphenylethylamine catabolic process
A0042420biological_processdopamine catabolic process
A0042428biological_processserotonin metabolic process
A0097621molecular_functionmonoamine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
AILE19
AGLY49
AGLY50
AARG51
ATHR52
AGLY66
AGLY67
AALA68
ATYR69
APRO243
AALA272
AGLY20
AILE273
ALEU277
ATRP397
ATYR402
ACYS406
ATYR407
AGLY434
ATHR435
AGLY443
ATYR444
AGLY22
AMET445
AALA448
AHOH704
AHOH711
AHOH717
AHOH723
AHOH725
AHOH726
AHOH727
AHOH762
AILE23
ASER24
ALEU42
AGLU43
AALA44
AARG45

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HRM A 700
ChainResidue
AILE180
AASN181
APHE208
AGLN215
AILE335
ALEU337
APHE352
ATYR407
ATYR444
AHOH726
AHOH746

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DCX A 1
ChainResidue
ATRP116
APRO118
ATYR121
ATHR509

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DCX A 2
ChainResidue
ATHR489
ATRP491

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AARG45
AASP46
AARG47
ALYS395
AGLU400
AHOH790

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 702
ChainResidue
ATYR62
AASP64
ATYR89
ALYS218
APHE219
AGLY222
AASP339
ALYS341
AHOH786
AHOH875

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3
ChainResidue
AASN75
ALEU78
AARG79
ALYS82
APRO476
ASER478
AASP480
AHOH802
AHOH879

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Anchor for type IV membrane protein"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsRegion: {"description":"Interaction with membrane phospholipid headgroups","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Important for substrate specificity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P21396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"S-8alpha-FAD cysteine","evidences":[{"source":"PubMed","id":"18391214","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BXR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BXS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z5X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Z5Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

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PDB entries from 2026-01-14

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