1OQ7
The crystal structure of the iron free (Apo-)form of 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 | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0009507 | cellular_component | chloroplast |
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 | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0009507 | cellular_component | chloroplast |
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 | 0006631 | biological_process | fatty acid metabolic process |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0009507 | cellular_component | chloroplast |
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 | 0006631 | biological_process | fatty acid metabolic process |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0009507 | cellular_component | chloroplast |
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 | 0006631 | biological_process | fatty acid metabolic process |
E | 0006633 | biological_process | fatty acid biosynthetic process |
E | 0009507 | cellular_component | chloroplast |
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 | 0006631 | biological_process | fatty acid metabolic process |
F | 0006633 | biological_process | fatty acid biosynthetic process |
F | 0009507 | cellular_component | chloroplast |
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 SR B 364 |
Chain | Residue |
A | GLU106 |
A | ASP148 |
B | GLU106 |
B | ASP148 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SR D 364 |
Chain | Residue |
C | GLU106 |
C | ASP148 |
D | GLU106 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SR E 364 |
Chain | Residue |
F | GLU106 |
E | GLU106 |
E | ASP148 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SR B 365 |
Chain | Residue |
A | ASP77 |
B | ASP77 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SR D 365 |
Chain | Residue |
C | ASP77 |
D | ASP77 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SR F 364 |
Chain | Residue |
E | ASP77 |
F | ASP77 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SR A 364 |
Chain | Residue |
B | ASP70 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SR C 364 |
Chain | Residue |
C | ASP70 |
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: BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937 |
Chain | Residue | Details |
A | GLU105 | |
B | GLU196 | |
B | GLU229 | |
B | HIS232 | |
C | GLU105 | |
C | GLU143 | |
C | HIS146 | |
C | GLU196 | |
C | GLU229 | |
C | HIS232 | |
D | GLU105 | |
A | GLU143 | |
D | GLU143 | |
D | HIS146 | |
D | GLU196 | |
D | GLU229 | |
D | HIS232 | |
E | GLU105 | |
E | GLU143 | |
E | HIS146 | |
E | GLU196 | |
E | GLU229 | |
A | HIS146 | |
E | HIS232 | |
F | GLU105 | |
F | GLU143 | |
F | HIS146 | |
F | GLU196 | |
F | GLU229 | |
F | HIS232 | |
A | GLU196 | |
A | GLU229 | |
A | HIS232 | |
B | GLU105 | |
B | GLU143 | |
B | HIS146 |
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 |