2XZ0

The Structure of the 2:1 (Partially Occupied) Complex Between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Acyl Carrier Protein.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
A	0016491	molecular_function	oxidoreductase activity
A	0045300	molecular_function	stearoyl-[ACP] desaturase activity
A	0046872	molecular_function	metal ion binding
B	0005515	molecular_function	protein binding
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
B	0016491	molecular_function	oxidoreductase activity
B	0045300	molecular_function	stearoyl-[ACP] desaturase activity
B	0046872	molecular_function	metal ion binding
C	0005515	molecular_function	protein binding
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0009507	cellular_component	chloroplast
C	0009536	cellular_component	plastid
C	0016491	molecular_function	oxidoreductase activity
C	0045300	molecular_function	stearoyl-[ACP] desaturase activity
C	0046872	molecular_function	metal ion binding
D	0000036	molecular_function	acyl carrier activity
D	0006633	biological_process	fatty acid biosynthetic process
D	0031177	molecular_function	phosphopantetheine binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 1364

Chain	Residue
A	GLU105
A	GLU143
A	HIS146
A	GLU229
A	FE1365

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 1365

Chain	Residue
A	HOH2009
A	GLU143
A	GLU196
A	GLU229
A	FE1364

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN A 1366

Chain	Residue
A	GLU106
B	ZN1366

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE B 1364

Chain	Residue
B	GLU105
B	GLU143
B	HIS146
B	GLU229
B	FE1365

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FE B 1365

Chain	Residue
B	TRP139
B	GLU143
B	GLU196
B	GLU229
B	HIS232
B	FE1364
B	HOH2001

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1366

Chain	Residue
A	ZN1366
B	GLU106
B	ASN144
B	ASP148

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 1367

Chain	Residue
B	PRO248
B	GLY315
B	SER317

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 1364

Chain	Residue
C	GLU105
C	GLU143
C	HIS146
C	GLU229
C	FE1365

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 1365

Chain	Residue
C	GLU143
C	GLU196
C	GLU229
C	FE1364
C	HOH2003

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ZN C 1366

Chain	Residue
C	GLU106
C	ASP148

---

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. KLGADSLDTVEIVMNL

Chain	Residue	Details
D	LYS33-LEU48

---

site_id	PS00574
Number of Residues	20
Details	FATTY_ACID_DESATUR_2 Fatty acid desaturases family 2 signature. SAvaqRLgvytakDYadILE

Chain	Residue	Details
A	SER283-GLU302

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12704186","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17088542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8861937","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16618110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	9
Details	M-CSA 136

Chain	Residue	Details
A	TRP62	hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
A	GLU105	metal ligand
A	GLU143	metal ligand
A	HIS146	hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
A	GLU196	metal ligand
A	THR199	electrostatic stabiliser, hydrogen bond donor
A	ASP228	hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
A	GLU229	metal ligand
A	HIS232	metal ligand

---

site_id	MCSA2
Number of Residues	9
Details	M-CSA 136

Chain	Residue	Details
B	TRP62	hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
B	GLU105	metal ligand
B	GLU143	metal ligand
B	HIS146	hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
B	GLU196	metal ligand
B	THR199	electrostatic stabiliser, hydrogen bond donor
B	ASP228	hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
B	GLU229	metal ligand
B	HIS232	metal ligand

---

site_id	MCSA3
Number of Residues	9
Details	M-CSA 136

Chain	Residue	Details
C	TRP62	hydrogen bond donor, single electron acceptor, single electron donor, single electron relay
C	GLU105	metal ligand
C	GLU143	metal ligand
C	HIS146	hydrogen bond donor, metal ligand, single electron acceptor, single electron donor, single electron relay
C	GLU196	metal ligand
C	THR199	electrostatic stabiliser, hydrogen bond donor
C	ASP228	hydrogen bond acceptor, single electron acceptor, single electron donor, single electron relay
C	GLU229	metal ligand
C	HIS232	metal ligand

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