Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OAC

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005509	molecular_function	calcium ion binding
A	0006559	biological_process	L-phenylalanine catabolic process
A	0008131	molecular_function	primary methylamine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0019607	biological_process	phenylethylamine catabolic process
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
A	0048038	molecular_function	quinone binding
A	0052595	molecular_function	aliphatic amine oxidase activity
B	0005507	molecular_function	copper ion binding
B	0005509	molecular_function	calcium ion binding
B	0006559	biological_process	L-phenylalanine catabolic process
B	0008131	molecular_function	primary methylamine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0019607	biological_process	phenylethylamine catabolic process
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
B	0048038	molecular_function	quinone binding
B	0052595	molecular_function	aliphatic amine oxidase activity

Functional Information from PDB Data

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

Chain	Residue
A	TPQ466
A	HIS524
A	HIS526
A	HIS689

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 802

Chain	Residue
A	LYS133
A	ASP533
A	LEU534
A	ASP535
A	ASP678
A	ALA679
A	HOH963

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 803

Chain	Residue
A	GLU573
A	TYR667
A	ASP670
A	GLU672
A	HOH992
A	HOH997

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 801

Chain	Residue
B	TPQ466
B	HIS524
B	HIS526
B	HIS689

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 802

Chain	Residue
B	LYS133
B	ASP533
B	LEU534
B	ASP535
B	ASP678
B	ALA679
B	HOH972

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 803

Chain	Residue
B	GLU573
B	TYR667
B	ASP670
B	GLU672
B	HOH1000
B	HOH1005

site_id	CUA
Number of Residues	4
Details	COPPER, BOUND IN THE ACTIVE SITE IN CHAIN A

Chain	Residue
A	TPQ466
A	HIS524
A	HIS526
A	HIS689

site_id	CUB
Number of Residues	4
Details	COPPER, BOUND IN THE ACTIVE SITE IN CHAIN B

Chain	Residue
B	TPQ466
B	HIS524
B	HIS526
B	HIS689

site_id	M1A
Number of Residues	6
Details	METAL BINDING SITE 1 IN CHAIN A. THE BOUND METAL IS THOUGHT TO BE CALCIUM

Chain	Residue
A	LEU534
A	ASP535
A	ASP678
A	ALA679
A	HOH963
A	ASP533

site_id	M1B
Number of Residues	6
Details	METAL BINDING SITE 1 IN CHAIN A. THE BOUND METAL IS THOUGHT TO BE CALCIUM

Chain	Residue
B	ASP533
B	LEU534
B	ASP535
B	ASP678
B	ALA679
B	HOH972

site_id	M2A
Number of Residues	6
Details	METAL BINDING SITE 2 IN CHAIN B. THE BOUND METAL IS THOUGHT TO BE CALCIUM

Chain	Residue
A	GLU573
A	TYR667
A	ASP670
A	GLU672
A	HOH992
A	HOH997

site_id	M2B
Number of Residues	6
Details	METAL BINDING SITE 2 IN CHAIN B. THE BOUND METAL IS THOUGHT TO BE CALCIUM

Chain	Residue
B	GLU573
B	TYR667
B	ASP670
B	GLU672
B	HOH1000
B	HOH1005

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU455-TYR468

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

Chain	Residue	Details
A	THR684-PRO697

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:10387067, ECO:0000269\|PubMed:9048544, ECO:0007744\|PDB:1OAC

Chain	Residue	Details
A	ASP383
B	ASP383

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Schiff-base intermediate with substrate; via topaquinone => ECO:0000269\|PubMed:10387067, ECO:0007744\|PDB:1OAC, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:2WGQ, ECO:0007744\|PDB:2WO0, ECO:0007744\|PDB:2WOF

Chain	Residue	Details
A	TPQ466
B	TPQ466

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10576737, ECO:0007744\|PDB:1D6U, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z

Chain	Residue	Details
A	TYR381
B	TYR381

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10576737, ECO:0000269\|PubMed:9048544, ECO:0007744\|PDB:1D6U, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z, ECO:0007744\|PDB:1LVN, ECO:0007744\|PDB:1SPU

Chain	Residue	Details
A	VAL463
B	VAL463

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10387067, ECO:0000269\|PubMed:10576737, ECO:0000269\|PubMed:9048544, ECO:0007744\|PDB:1D6U, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z, ECO:0007744\|PDB:1DYU, ECO:0007744\|PDB:1JRQ, ECO:0007744\|PDB:1LVN, ECO:0007744\|PDB:1OAC, ECO:0007744\|PDB:1QAF, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:1QAL, ECO:0007744\|PDB:1SPU, ECO:0007744\|PDB:2W0Q, ECO:0007744\|PDB:2WGQ, ECO:0007744\|PDB:2WO0, ECO:0007744\|PDB:2WOF, ECO:0007744\|PDB:2WOH

Chain	Residue	Details
A	HIS524
A	HIS526
A	HIS689
B	HIS524
B	HIS526
B	HIS689

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q43077

Chain	Residue	Details
A	ASP533
A	ASP535
A	ASP678
B	ASP533
B	ASP535
B	ASP678

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10387067, ECO:0000269\|PubMed:10576737, ECO:0000269\|PubMed:9048544, ECO:0007744\|PDB:1D6U, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z, ECO:0007744\|PDB:1DYU, ECO:0007744\|PDB:1JRQ, ECO:0007744\|PDB:1LVN, ECO:0007744\|PDB:1OAC, ECO:0007744\|PDB:1QAF, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:1QAL, ECO:0007744\|PDB:1SPU, ECO:0007744\|PDB:2W0Q, ECO:0007744\|PDB:2WGQ, ECO:0007744\|PDB:2WOH

Chain	Residue	Details
A	LEU534
B	LEU534

site_id	SWS_FT_FI8
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10387067, ECO:0000269\|PubMed:10576737, ECO:0000269\|PubMed:9048544, ECO:0007744\|PDB:1D6U, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z, ECO:0007744\|PDB:1DYU, ECO:0007744\|PDB:1JRQ, ECO:0007744\|PDB:1LVN, ECO:0007744\|PDB:1OAC, ECO:0007744\|PDB:1QAF, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:1QAL, ECO:0007744\|PDB:1SPU, ECO:0007744\|PDB:2W0Q, ECO:0007744\|PDB:2WGQ

Chain	Residue	Details
A	GLU573
A	TYR667
A	GLU672
B	GLU573
B	TYR667
B	GLU672

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:10576737, ECO:0007744\|PDB:1D6Y, ECO:0007744\|PDB:1D6Z, ECO:0007744\|PDB:1DYU, ECO:0007744\|PDB:1OAC, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:1QAL, ECO:0007744\|PDB:2WGQ

Chain	Residue	Details
A	ASP670
B	ASP670

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	ALA679
B	ALA679

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0000269\|PubMed:10387067, ECO:0007744\|PDB:1DYU, ECO:0007744\|PDB:1JRQ, ECO:0007744\|PDB:1QAF, ECO:0007744\|PDB:1QAK, ECO:0007744\|PDB:1QAL

Chain	Residue	Details
A	TPQ466
B	TPQ466

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details

Chain	Residue	Details
A	ASP383
A	TPQ466

site_id	CSA2
Number of Residues	1
Details

Chain	Residue	Details
B	ASP383

site_id	MCSA1
Number of Residues	6
Details	M-CSA 864

Chain	Residue	Details
A	TYR369	electrostatic stabiliser
A	ASP383	proton shuttle (general acid/base)
A	TPQ466	covalent catalysis
A	HIS524	metal ligand
A	HIS526	metal ligand
A	HIS689	metal ligand

site_id	MCSA2
Number of Residues	6
Details	M-CSA 864

Chain	Residue	Details
B	TYR369	electrostatic stabiliser
B	ASP383	proton shuttle (general acid/base)
B	TPQ466	covalent catalysis
B	HIS524	metal ligand
B	HIS526	metal ligand
B	HIS689	metal ligand

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