Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OQB

The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).

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	0005515	molecular_function	protein binding
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0009507	cellular_component	chloroplast
D	0009536	cellular_component	plastid
D	0016491	molecular_function	oxidoreductase activity
D	0045300	molecular_function	stearoyl-[ACP] desaturase activity
D	0046872	molecular_function	metal ion binding
E	0005515	molecular_function	protein binding
E	0006629	biological_process	lipid metabolic process
E	0006631	biological_process	fatty acid metabolic process
E	0006633	biological_process	fatty acid biosynthetic process
E	0009507	cellular_component	chloroplast
E	0009536	cellular_component	plastid
E	0016491	molecular_function	oxidoreductase activity
E	0045300	molecular_function	stearoyl-[ACP] desaturase activity
E	0046872	molecular_function	metal ion binding
F	0005515	molecular_function	protein binding
F	0006629	biological_process	lipid metabolic process
F	0006631	biological_process	fatty acid metabolic process
F	0006633	biological_process	fatty acid biosynthetic process
F	0009507	cellular_component	chloroplast
F	0009536	cellular_component	plastid
F	0016491	molecular_function	oxidoreductase activity
F	0045300	molecular_function	stearoyl-[ACP] desaturase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 A 364

Chain	Residue
A	GLU105
A	GLU143
A	HIS146
A	GLU229

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 B 364

Chain	Residue
B	GLU105
B	GLU143
B	HIS146
B	GLU229

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 C 364

Chain	Residue
C	GLU143
C	HIS146
C	GLU229
C	GLU105

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 D 364

Chain	Residue
D	GLU105
D	GLU143
D	HIS146
D	GLU229

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 E 364

Chain	Residue
E	GLU105
E	GLU143
E	HIS146
E	GLU229

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE2 F 364

Chain	Residue
F	GLU105
F	GLU143
F	HIS146
F	GLU229

Functional Information from PROSITE/UniProt

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	36
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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1afr

Chain	Residue	Details
A	THR199
A	ASP228
A	TRP62
A	HIS146

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1afr

Chain	Residue	Details
B	THR199
B	ASP228
B	TRP62
B	HIS146

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

Chain	Residue	Details
C	THR199
C	ASP228
C	TRP62
C	HIS146

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

Chain	Residue	Details
D	THR199
D	ASP228
D	TRP62
D	HIS146

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1afr

Chain	Residue	Details
E	THR199
E	ASP228
E	TRP62
E	HIS146

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1afr

Chain	Residue	Details
F	THR199
F	ASP228
F	TRP62
F	HIS146

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

site_id	MCSA4
Number of Residues	9
Details	M-CSA 136

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

site_id	MCSA5
Number of Residues	9
Details	M-CSA 136

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

site_id	MCSA6
Number of Residues	9
Details	M-CSA 136

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

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