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4KFE

Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 7.0

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
D0005507molecular_functioncopper ion binding
D0005777cellular_componentperoxisome
D0008131molecular_functionprimary methylamine oxidase activity
D0009308biological_processamine metabolic process
D0016491molecular_functionoxidoreductase activity
D0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
D0046872molecular_functionmetal ion binding
D0048038molecular_functionquinone binding
E0005507molecular_functioncopper ion binding
E0005777cellular_componentperoxisome
E0008131molecular_functionprimary methylamine oxidase activity
E0009308biological_processamine metabolic process
E0016491molecular_functionoxidoreductase activity
E0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
E0046872molecular_functionmetal ion binding
E0048038molecular_functionquinone binding
F0005507molecular_functioncopper ion binding
F0005777cellular_componentperoxisome
F0008131molecular_functionprimary methylamine oxidase activity
F0009308biological_processamine metabolic process
F0016491molecular_functionoxidoreductase activity
F0016641molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
F0046872molecular_functionmetal ion binding
F0048038molecular_functionquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 801
ChainResidue
AHIS456
AHIS458
AHIS624
APEO802

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO A 802
ChainResidue
AMET634
ACU801
AHOH1055
ATYY405
ALEU429
AHIS456
AHIS458
AHIS624

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FOR A 803
ChainResidue
ATRP156
AASP319
ATYR323
ATYY405

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 804
ChainResidue
AGLN66
AGLN70
AGLY72
AHOH955
AHOH1353
FTYR534
FGLU651

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 805
ChainResidue
ALYS214
AVAL215
AGLY435
AASP436
AASN450
AHOH1133

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 806
ChainResidue
AGLU368
ALYS393
ATYR410
AASP422
AARG424
AHOH1072
AHOH1542
BGLY371

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 807
ChainResidue
APRO484
ATYR485
AHOH1636

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 808
ChainResidue
AHIS218
ALYS219
ATYR448
AHOH1185

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 809
ChainResidue
ATYR160
ALYS561
ASER591
AHOH1246
FLYS561
FASP593
FGOL811
FHOH994

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 810
ChainResidue
AGLU110
AHOH1149
AHOH1509
FALA133
FILE204
FILE206

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 811
ChainResidue
ALYS68
FHOH1601

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 812
ChainResidue
AGLY142
APRO144
AGLU147
ATYR177
AHOH1624
EHOH1357

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 813
ChainResidue
AARG61
AILE65
AASP471
AASP613
AHOH1327
AHOH1610

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 814
ChainResidue
AASP131
AALA133
AVAL203
AILE204
AHOH1645
FGLU110
FHOH1432

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 815
ChainResidue
APRO59
AARG61
AHIS294
ATYR575
AASN578
AHOH911
AHOH1141
AHOH1305
AHOH1406

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 816
ChainResidue
ASER251
ALYS253
AGLU260
ATRP261
ASER262
AHOH1192
AHOH1257

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 801
ChainResidue
BHIS456
BHIS458
BHIS624
BPEO802

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO B 802
ChainResidue
BTYY405
BLEU429
BHIS456
BHIS458
BHIS624
BMET634
BCU801
BHOH1094

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FOR B 803
ChainResidue
BTRP156
BTYR323
BTYY405

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 804
ChainResidue
AGLY371
BGLU368
BLYS393
BVAL412
BASP422
BHOH1028
BHOH1472
BHOH1496

site_idCC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 805
ChainResidue
BGLU58
BPRO59
BHIS294
BTYR575
BASN578
BHOH907
BHOH1037
BHOH1049
BHOH1285

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 806
ChainResidue
BPRO484
BTYR499
BHOH1630

site_idCC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 807
ChainResidue
ATYR534
BHIS218
BLYS219
BTYR448
BPRO449
BPO4812
BHOH1593

site_idCC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 808
ChainResidue
BLEU558
BLYS561
BSER591
BGOL809
BHOH988
BHOH1394
CLYS561
CASP593

site_idCC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 809
ChainResidue
BLYS561
BASP593
BGOL808
BHOH988
BHOH1487
CTYR160
CLYS561
CSER591
CHOH1512

site_idCC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 810
ChainResidue
BARG61
BILE65
BASP471
BASP613
BHOH1592

site_idCC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 811
ChainResidue
BARG213
BLYS214
BVAL215
BASP436
BASN450
BHOH1021
BHOH1617

site_idDC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 812
ChainResidue
BHIS218
BLYS219
BGOL807

site_idDC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 813
ChainResidue
BPRO144
BGLU147
BTYR177
BHOH1146
DHOH1410

site_idDC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 801
ChainResidue
CHIS456
CHIS458
CHIS624
CPEO802
CHOH1426

site_idDC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO C 802
ChainResidue
CTYY405
CHIS456
CHIS458
CHIS624
CMET634
CCU801
CHOH990
CHOH1426

site_idDC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 803
ChainResidue
CHIS23
CTYR64
CLYS68
CASP280
CHOH964
CHOH1521

site_idDC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 804
ChainResidue
CLYS214
CVAL215
CASP436
CHOH1116
CHOH1256

site_idDC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL C 805
ChainResidue
BLYS68

site_idDC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 806
ChainResidue
CLYS393
CVAL412
CASP422
CHOH1033
CHOH1562

site_idDC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL C 807
ChainResidue
CTYR499
DPRO442

site_idEC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 C 808
ChainResidue
CHIS218
CLYS219

site_idEC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL C 809
ChainResidue
BGLN66
BGLN70
BGLY72
CTYR534
CGLU651
CHOH942
CHOH1487
DLYS231

site_idEC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 810
ChainResidue
CARG57
CTYR80
CASN578
CTYR581
CASP585
CHOH1146
CHOH1262
CHOH1363
CHOH1495

site_idEC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO D 701
ChainResidue
DTYY405
DLEU429
DHIS456
DHIS458
DHIS624
DMET634
DCU703
DHOH805

site_idEC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FOR D 702
ChainResidue
DTRP156
DASP319
DTYR323
DTYY405

site_idEC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU D 703
ChainResidue
DHIS456
DHIS458
DHIS624
DPEO701
DHOH1351

site_idEC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 704
ChainResidue
DGLY142
DPRO144
DGLU147
DTYR177
DLYS217
DHOH1127
DHOH1466

site_idEC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL D 705
ChainResidue
DLYS150

site_idEC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL D 706
ChainResidue
DTYR499

site_idFC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL D 707
ChainResidue
BLYS62
BALA63
BGLN66
BPRO73
BHOH1007
BHOH1345
BHOH1581
DLYS231
DVAL232
DGLY233

site_idFC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 708
ChainResidue
DGLU368
DLYS393
DVAL412
DASP422
DARG424
DHOH998
DHOH1429

site_idFC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 709
ChainResidue
DHIS23
DTYR64
DLYS68
DLYS265
DASP280
DHOH909

site_idFC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL D 710
ChainResidue
DTRP67
DLYS68

site_idFC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 711
ChainResidue
DLEU56
DARG57
DTYR80
DLEU580
DHOH993
DHOH1089
DHOH1487

site_idFC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 712
ChainResidue
DPHE252
DLYS253
DMET254
DILE342
DHIS343

site_idFC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU E 801
ChainResidue
EHIS456
EHIS458
EHIS624
EPEO802
EHOH1432

site_idFC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO E 802
ChainResidue
ETYY405
ELEU429
EHIS456
EHIS458
EHIS624
EMET634
ECU801
EHOH903

site_idFC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 803
ChainResidue
EGLY142
EPRO144
EGLU147
ETYR177
ELYS217
EHOH1248

site_idGC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL E 804
ChainResidue
EPHE252
ELYS253
EMET254
EILE342
EHIS343
EHOH1486

site_idGC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL E 805
ChainResidue
EGLU58
EPRO59
EARG295
ETYR575
EASP577
EASN578
EHOH948
EHOH957
EHOH1477
EHOH1502

site_idGC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL E 806
ChainResidue
EHIS23
ETYR64
ELYS68
ELYS265
EASP280

site_idGC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL E 807
ChainResidue
EGLU368
ELYS393
EARG420
EASP422
EARG424
EHOH1036
EHOH1308
EHOH1441
FGLY371

site_idGC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU F 801
ChainResidue
FHIS456
FHIS458
FHIS624
FPEO802
FHOH1395

site_idGC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEO F 802
ChainResidue
FTYY405
FHIS456
FHIS458
FHIS624
FMET634
FCU801
FHOH983
FHOH1395

site_idGC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL F 803
ChainResidue
FHIS23
FTYR64
FLYS68
FLYS265
FASP280
FHOH946

site_idGC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL F 804
ChainResidue
EGLY371
FLYS393
FVAL412
FASP422
FARG424
FGOL805
FHOH1036
FHOH1525

site_idGC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL F 805
ChainResidue
EGLY371
EARG390
FCYS338
FLYS339
FHIS366
FGLU368
FGOL804
FHOH1334

site_idHC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL F 806
ChainResidue
EPRO484
FPRO442

site_idHC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL F 807
ChainResidue
FPHE252
FLYS253
FMET254
FHIS343
FHOH1203

site_idHC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL F 808
ChainResidue
FPRO484

site_idHC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 F 809
ChainResidue
FHIS218
FLYS219
FHOH1528

site_idHC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL F 810
ChainResidue
FLEU512
FASP604
FGLY605
FHOH1069
FHOH1375
FHOH1596

site_idHC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL F 811
ChainResidue
ALYS561
AASP593
AGOL809
FTYR160
FLEU558
FLYS561
FSER591
FHOH994
FHOH1489

site_idHC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL F 812
ChainResidue
FGLU58
FPRO59
FTYR575
FASN578
FHOH924
FHOH987
FHOH1182

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 Residues6
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
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 Residues66
DetailsBinding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues18
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_FI5
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
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_FI7
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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