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3NBB

Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha

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 701
ChainResidue
ATY8405
AHIS456
AHIS458
AHIS624

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 701
ChainResidue
BTY8405
BHIS456
BHIS458
BHIS624

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 701
ChainResidue
CHIS456
CHIS458
CHIS624
CTY8405

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 701
ChainResidue
DTY8405
DHIS456
DHIS458
DHIS624

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU E 701
ChainResidue
ETY8405
EHIS456
EHIS458
EHIS624

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU F 701
ChainResidue
FTY8405
FHIS456
FHIS458
FHIS624

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
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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