3DY5

Allene oxide synthase 8R-lipoxygenase from Plexaura homomalla

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0006631	biological_process	fatty acid metabolic process
A	0016020	cellular_component	membrane
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0019369	biological_process	arachidonate metabolic process
A	0020037	molecular_function	heme binding
A	0034440	biological_process	lipid oxidation
A	0046872	molecular_function	metal ion binding
A	0047677	molecular_function	arachidonate 8(R)-lipoxygenase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0006631	biological_process	fatty acid metabolic process
C	0016020	cellular_component	membrane
C	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C	0019369	biological_process	arachidonate metabolic process
C	0020037	molecular_function	heme binding
C	0034440	biological_process	lipid oxidation
C	0046872	molecular_function	metal ion binding
C	0047677	molecular_function	arachidonate 8(R)-lipoxygenase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 A 1099

Chain	Residue
A	HIS757
A	HIS762
A	HIS943
A	ASN947
A	ILE1066

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 C 1099

Chain	Residue
C	ILE1066
C	HIS757
C	HIS762
C	HIS943
C	ASN947

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM A 1100

Chain	Residue
A	PHE53
A	ARG64
A	ALA65
A	THR66
A	HIS67
A	ARG102
A	SER118
A	SER120
A	VAL135
A	MET136
A	ASN137
A	SER194
A	GLN195
A	PHE322
A	ARG349
A	VAL352
A	TYR353
A	GLN357
A	ARG360

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 1100

Chain	Residue
C	PHE53
C	ARG64
C	ALA65
C	THR66
C	HIS67
C	ARG102
C	SER118
C	SER120
C	VAL135
C	MET136
C	ASN137
C	SER194
C	GLN195
C	PHE322
C	ARG349
C	VAL352
C	TYR353
C	GLN357
C	ARG360

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16162493","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1lnh

Chain	Residue	Details
A	ASN947

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1lnh

Chain	Residue	Details
C	ASN947

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1lnh

Chain	Residue	Details
A	TYR193
A	ASN137
A	THR66
A	HIS67

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1lnh

Chain	Residue	Details
C	TYR193
C	ASN137
C	THR66
C	HIS67

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 758

Chain	Residue	Details
A	THR66	electrostatic stabiliser
A	HIS67	electrostatic stabiliser, proton acceptor, proton donor
A	ASN137	electrostatic stabiliser
A	TYR353	metal ligand

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 758

Chain

Residue

Details

---