Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KFF

Crystal structure of Hansenula polymorpha copper amine oxidase-1 reduced by methylamine at pH 8.5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005777	cellular_component	peroxisome
A	0008131	molecular_function	primary methylamine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
A	0046872	molecular_function	metal ion binding
A	0048038	molecular_function	quinone binding
B	0005507	molecular_function	copper ion binding
B	0005777	cellular_component	peroxisome
B	0008131	molecular_function	primary methylamine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
B	0046872	molecular_function	metal ion binding
B	0048038	molecular_function	quinone binding
C	0005507	molecular_function	copper ion binding
C	0005777	cellular_component	peroxisome
C	0008131	molecular_function	primary methylamine oxidase activity
C	0009308	biological_process	amine metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016641	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
C	0046872	molecular_function	metal ion binding
C	0048038	molecular_function	quinone binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 801

Chain	Residue
A	TYY405
A	HIS456
A	HIS458
A	HIS624

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 802

Chain	Residue
A	HOH1187
A	GLU368
A	LYS393
A	ASP422
A	ARG424
A	HOH984

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	GLY142
A	GLU147
A	TYR177
A	SER216
B	HOH1271

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 804

Chain	Residue
A	HIS218
A	LYS219
A	TYR448
A	TYR534

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 805

Chain	Residue
A	GLU58
A	PRO59
A	TYR575
A	ASN578
A	HOH907
A	HOH963
A	HOH1318

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 806

Chain	Residue
A	PRO442
A	PRO484
A	TYR485
A	TYR499

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 807

Chain	Residue
A	TRP67
A	LYS68

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 808

Chain	Residue
A	GLN66
A	GLN70
A	GLY72
A	PRO73
C	TYR534
C	GLU651
C	HOH872

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 801

Chain	Residue
B	TYY405
B	HIS456
B	HIS458
B	HIS624

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 802

Chain	Residue
B	GLU368
B	LYS393
B	TYR410
B	ASP422
B	ARG424
B	HOH1100
B	HOH1104

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 803

Chain	Residue
B	HIS23
B	TYR64
B	LYS68
B	LYS265
B	HIS267
B	ASP280
B	HOH982

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 804

Chain	Residue
B	PRO484
C	PRO442

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL C 701

Chain	Residue
C	PRO484
C	TYR499

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 702

Chain	Residue
C	TYY405
C	HIS456
C	HIS458
C	HIS624

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 703

Chain	Residue
C	HIS23
C	TYR64
C	LYS68
C	LYS265
C	ASP280
C	HOH912

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 704

Chain	Residue
A	GLY594
A	HOH1105
A	HOH1257
B	HOH1072
C	ARG163
C	PHE310
C	HOH1017

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 705

Chain	Residue
C	LYS393
C	ASP422
C	ARG424
C	HOH1087

Functional Information from PROSITE/UniProt

site_id	PS01159
Number of Residues	26
Details	WW_DOMAIN_1 WW/rsp5/WWP domain signature. WgtgkrlqqalvYYrsdedd.SQYSHP

Chain	Residue	Details
A	TRP164-PRO189

site_id	PS01164
Number of Residues	14
Details	COPPER_AMINE_OXID_1 Copper amine oxidase topaquinone signature. LVVsqifTaaNYEY

Chain	Residue	Details
A	LEU394-TYR407

site_id	PS01165
Number of Residues	14
Details	COPPER_AMINE_OXID_2 Copper amine oxidase copper-binding site signature. TfGitHFpapEDfP

Chain	Residue	Details
A	THR619-PRO632

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	33
Details	Binding site: {"evidences":[{"source":"PDB","id":"4EV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EV5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	9
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43077","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Modified 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9551552","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)