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3NBJ

Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005777cellular_componentperoxisome
A0008131molecular_functionprimary amine oxidase activity
A0009308biological_processamine metabolic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0048038molecular_functionquinone binding
A0052595molecular_functionaliphatic amine oxidase activity
B0005507molecular_functioncopper ion binding
B0005777cellular_componentperoxisome
B0008131molecular_functionprimary amine oxidase activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0048038molecular_functionquinone binding
B0052595molecular_functionaliphatic amine oxidase activity
C0005507molecular_functioncopper ion binding
C0005777cellular_componentperoxisome
C0008131molecular_functionprimary amine oxidase activity
C0009308biological_processamine metabolic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0048038molecular_functionquinone binding
C0052595molecular_functionaliphatic amine oxidase activity
D0005507molecular_functioncopper ion binding
D0005777cellular_componentperoxisome
D0008131molecular_functionprimary amine oxidase activity
D0009308biological_processamine metabolic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0048038molecular_functionquinone binding
D0052595molecular_functionaliphatic amine oxidase activity
E0005507molecular_functioncopper ion binding
E0005777cellular_componentperoxisome
E0008131molecular_functionprimary amine oxidase activity
E0009308biological_processamine metabolic process
E0016491molecular_functionoxidoreductase activity
E0046872molecular_functionmetal ion binding
E0048038molecular_functionquinone binding
E0052595molecular_functionaliphatic amine oxidase activity
F0005507molecular_functioncopper ion binding
F0005777cellular_componentperoxisome
F0008131molecular_functionprimary amine oxidase activity
F0009308biological_processamine metabolic process
F0016491molecular_functionoxidoreductase activity
F0046872molecular_functionmetal ion binding
F0048038molecular_functionquinone binding
F0052595molecular_functionaliphatic amine oxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 701
ChainResidue
ATY8405
AHIS456
AHIS458
AHIS624

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 702
ChainResidue
APRO209
AASN210
AARG211
AHOH1250
AHOH1373

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 703
ChainResidue
AHIS218
ALYS219

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
AGLY594
AVAL595
AARG596
AHOH1324
AHOH1393

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 701
ChainResidue
BTY8405
BHIS456
BHIS458
BHIS624

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 702
ChainResidue
BPRO209
BASN210
BARG211
BHOH1250
BHOH1373

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 703
ChainResidue
BHIS218
BLYS219

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 704
ChainResidue
BGLY594
BVAL595
BARG596
BHOH1324
BHOH1393

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 701
ChainResidue
CTY8405
CHIS456
CHIS458
CHIS624

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 702
ChainResidue
CPRO209
CASN210
CARG211
CHOH1250
CHOH1373

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 C 703
ChainResidue
CHIS218
CLYS219

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 C 704
ChainResidue
CGLY594
CVAL595
CARG596
CHOH1324
CHOH1393

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 701
ChainResidue
DTY8405
DHIS456
DHIS458
DHIS624

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 D 702
ChainResidue
DPRO209
DASN210
DARG211
DHOH1250
DHOH1373

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 D 703
ChainResidue
DHIS218
DLYS219

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 D 704
ChainResidue
DGLY594
DVAL595
DARG596
DHOH1324
DHOH1393

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU E 701
ChainResidue
ETY8405
EHIS456
EHIS458
EHIS624

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 E 702
ChainResidue
EPRO209
EASN210
EARG211
EHOH1250
EHOH1373

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 E 703
ChainResidue
EHIS218
ELYS219

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 E 704
ChainResidue
EGLY594
EVAL595
EARG596
EHOH1324
EHOH1393

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU F 701
ChainResidue
FTY8405
FHIS456
FHIS458
FHIS624

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 F 702
ChainResidue
FPRO209
FASN210
FARG211
FHOH1250
FHOH1373

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 F 703
ChainResidue
FHIS218
FLYS219

site_idCC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 F 704
ChainResidue
FGLY594
FVAL595
FARG596
FHOH1324
FHOH1393

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

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
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552
ChainResidueDetails
AASP319
BASP319
CASP319
DASP319
EASP319
FASP319

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF
ChainResidueDetails
ATY8405
BTY8405
CTY8405
DTY8405
ETY8405
FTY8405

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5
ChainResidueDetails
AALA317
BALA317
CALA317
DALA317
EALA317
FALA317

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46883
ChainResidueDetails
AALA402
BALA402
CALA402
DALA402
EALA402
FALA402

site_idSWS_FT_FI5
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV, ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H, ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ, ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD, ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF
ChainResidueDetails
AHIS456
DHIS456
DHIS458
DHIS624
EHIS456
EHIS458
EHIS624
FHIS456
FHIS458
FHIS624
AHIS458
AHIS624
BHIS456
BHIS458
BHIS624
CHIS456
CHIS458
CHIS624

site_idSWS_FT_FI6
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q43077
ChainResidueDetails
AASP465
DASP465
DASP613
DILE614
EASP465
EASP613
EILE614
FASP465
FASP613
FILE614
AASP613
AILE614
BASP465
BASP613
BILE614
CASP465
CASP613
CILE614

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE
ChainResidueDetails
ATY8405
BTY8405
CTY8405
DTY8405
ETY8405
FTY8405

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552
ChainResidueDetails
AASN243
BASN243
CASN243
DASN243
EASN243
FASN243

223532

PDB entries from 2024-08-07

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