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1W2Z

PSAO and Xenon

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0008131molecular_functionprimary amine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
A0052597molecular_functiondiamine oxidase activity
B0005507molecular_functioncopper ion binding
B0008131molecular_functionprimary amine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
B0052595molecular_functionaliphatic amine oxidase activity
B0052597molecular_functiondiamine oxidase activity
C0005507molecular_functioncopper ion binding
C0008131molecular_functionprimary amine oxidase activity
C0009308biological_processamine metabolic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0048038molecular_functionquinone binding
C0052595molecular_functionaliphatic amine oxidase activity
C0052597molecular_functiondiamine oxidase activity
D0005507molecular_functioncopper ion binding
D0008131molecular_functionprimary amine oxidase activity
D0009308biological_processamine metabolic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0048038molecular_functionquinone binding
D0052595molecular_functionaliphatic amine oxidase activity
D0052597molecular_functiondiamine oxidase activity
Functional Information from PROSITE/UniProt
site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LIVrtivTvgNYDN
ChainResidueDetails
ALEU376-ASN389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
AASP300
BASP300
CASP300
DASP300

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
ATPQ387
BTPQ387
CTPQ387
DTPQ387

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12807
ChainResidueDetails
APHE298
BPHE298
CPHE298
DPHE298

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46883
ChainResidueDetails
AVAL384
BVAL384
CVAL384
DVAL384

site_idSWS_FT_FI5
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:8805580, ECO:0007744|PDB:1KSI
ChainResidueDetails
AHIS442
BHIS444
BASP451
BPHE452
BASP453
BASP592
BILE593
BHIS603
CHIS442
CHIS444
CASP451
AHIS444
CPHE452
CASP453
CASP592
CILE593
CHIS603
DHIS442
DHIS444
DASP451
DPHE452
DASP453
AASP451
DASP592
DILE593
DHIS603
APHE452
AASP453
AASP592
AILE593
AHIS603
BHIS442

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:8805580, ECO:0007744|PDB:1KSI
ChainResidueDetails
ATPQ387
BTPQ387
CTPQ387
DTPQ387

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8805580, ECO:0007744|PDB:1KSI
ChainResidueDetails
AASN131
BASN131
CASN131
DASN131

site_idSWS_FT_FI8
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN364
BASN364
CASN364
DASN364

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
AASP300

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
BASP300

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
CASP300

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oac
ChainResidueDetails
DASP300

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PDB entries from 2024-07-24

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