1EKM

CRYSTAL STRUCTURE AT 2.5 A RESOLUTION OF ZINC-SUBSTITUTED COPPER AMINE OXIDASE OF HANSENULA POLYMORPHA EXPRESSED IN ESCHERICHIA COLI

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 amine oxidase activity
A	0009308	biological_process	amine metabolic process
A	0016491	molecular_function	oxidoreductase activity
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	0005777	cellular_component	peroxisome
B	0008131	molecular_function	primary amine oxidase activity
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
B	0048038	molecular_function	quinone binding
B	0052595	molecular_function	aliphatic amine oxidase activity
C	0005507	molecular_function	copper ion binding
C	0005777	cellular_component	peroxisome
C	0008131	molecular_function	primary amine oxidase activity
C	0009308	biological_process	amine metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0048038	molecular_function	quinone binding
C	0052595	molecular_function	aliphatic amine oxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 701

Chain	Residue
A	TYR405
A	HIS456
A	HIS458
A	HIS624

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 701

Chain	Residue
B	TYR405
B	HIS456
B	HIS458
B	HIS624

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 701

Chain	Residue
C	HIS456
C	HIS458
C	HIS624
C	TYR405

---

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	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9551552

Chain	Residue	Details
A	ASP319
B	ASP319
C	ASP319

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_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

Chain	Residue	Details
A	TYR405
B	TYR405
C	TYR405

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5

Chain	Residue	Details
A	ALA317
B	ALA317
C	ALA317

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P46883

Chain	Residue	Details
A	ALA402
B	ALA402
C	ALA402

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	BINDING: 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

Chain	Residue	Details
A	HIS456
A	HIS458
A	HIS624
B	HIS456
B	HIS458
B	HIS624
C	HIS456
C	HIS458
C	HIS624

---

site_id	SWS_FT_FI6
Number of Residues	9
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q43077

Chain	Residue	Details
A	ASP465
A	ASP613
A	ILE614
B	ASP465
B	ASP613
B	ILE614
C	ASP465
C	ASP613
C	ILE614

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: 2',4',5'-topaquinone => ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE

Chain	Residue	Details
A	TYR405
B	TYR405
C	TYR405

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9551552

Chain	Residue	Details
A	ASN243
B	ASN243
C	ASN243

---