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3T0U

Hansenula polymorpha copper amine oxidase-1 in complex with Cu(I)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005777cellular_componentperoxisome
A0008131molecular_functionprimary methylamine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
B0005507molecular_functioncopper ion binding
B0005777cellular_componentperoxisome
B0008131molecular_functionprimary methylamine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
C0005507molecular_functioncopper ion binding
C0005777cellular_componentperoxisome
C0008131molecular_functionprimary methylamine oxidase activity
C0009308biological_processamine metabolic process
C0016491molecular_functionoxidoreductase activity
C0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
C0046872molecular_functionmetal ion binding
C0048038molecular_functionquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU1 A 801
ChainResidue
ATYR405
ALEU425
AHIS456
AHIS458
AHIS624

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 802
ChainResidue
AASP280
AHOH1162
AHIS23
ATYR64
ALYS68
ALYS265

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 803
ChainResidue
APRO484
ATYR485
ATYR499
AHOH1413

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 804
ChainResidue
ATRP67
ALYS68

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
ALYS393
AARG420
AASP422
AARG424
AHOH969
AHOH1158
AHOH1300
AHOH1516
BGLY371

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 806
ChainResidue
ALYS561
ALYS561
ASER591
AASP593
AHOH1241
AHOH1241

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU1 B 801
ChainResidue
BTYR405
BLEU425
BHIS456
BHIS458
BHIS624

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 802
ChainResidue
BTYR534
BHOH1001
BHOH1461
CGLN66
CGLN70
CGLY72

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 803
ChainResidue
BHIS23
BTYR64
BLYS68
BLYS265
BASP280
BHOH1065
BHOH1692

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 804
ChainResidue
BHIS218
BLYS219

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL B 805
ChainResidue
CTRP67

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 806
ChainResidue
BLYS214
BVAL215
BASP436
BHOH1307

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 807
ChainResidue
APRO442
BPRO484
BTYR485
BHOH1371
BHOH1424

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 808
ChainResidue
BLYS561
BSER591
BHOH1392
CLYS561
CASP593
CGOL805
CHOH1022

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 C 801
ChainResidue
CTYR405
CHIS456
CHIS458
CHIS624

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 802
ChainResidue
CPRO442
CPRO484
CTYR485
CHOH1424
CHOH1656

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 803
ChainResidue
AHOH1432
CARG61
CLYS62
CGLN70
CASP471
CASP613
CHOH1648
CHOH1783
CHOH1798

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 804
ChainResidue
CGLY371
CLYS393
CVAL412
CASP422
CARG424
CHOH923
CHOH1110
CHOH1765

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL C 805
ChainResidue
CSER591
CHOH1022
CHOH1333
BLYS561
BASP593
BGOL808
CLYS561

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 806
ChainResidue
CHIS23
CTYR64
CLYS68
CLYS265
CASP280
CHOH1092

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 807
ChainResidue
CHIS218
CLYS219
CTYR448
CTYR534

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 808
ChainResidue
CLYS214
CVAL215
CGLY435
CASP436

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 809
ChainResidue
CGLY142
CPRO144
CGLU147
CTYR177
CHOH1258

Functional Information from PROSITE/UniProt
site_idPS01159
Number of Residues26
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP
ChainResidueDetails
ATRP164-PRO189

site_idPS01164
Number of Residues14
DetailsCOPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY
ChainResidueDetails
ALEU394-TYR407

site_idPS01165
Number of Residues14
DetailsCOPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP
ChainResidueDetails
ATHR619-PRO632

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P46883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10933787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EKM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OOV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N9H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T0U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KFF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"2',4',5'-topaquinone","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OQE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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