1OQ4
The Crystal Structure of the Complex between Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean) and Azide.
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 | 5 |
Details | BINDING SITE FOR RESIDUE FE A 364 |
Chain | Residue |
A | GLU105 |
A | GLU143 |
A | HIS146 |
A | GLU229 |
A | AZI366 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 365 |
Chain | Residue |
A | AZI366 |
A | GLU143 |
A | GLU196 |
A | GLU229 |
A | HIS232 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE AZI A 366 |
Chain | Residue |
A | GLU105 |
A | GLU143 |
A | GLU196 |
A | THR199 |
A | FE364 |
A | FE365 |
A | HOH442 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE B 364 |
Chain | Residue |
B | GLU105 |
B | GLU143 |
B | HIS146 |
B | GLU229 |
B | AZI1366 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE B 365 |
Chain | Residue |
B | GLU143 |
B | GLU196 |
B | GLU229 |
B | HIS232 |
B | AZI1366 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE AZI B 1366 |
Chain | Residue |
B | GLU105 |
B | GLU143 |
B | GLU196 |
B | THR199 |
B | FE364 |
B | FE365 |
B | HOH1442 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE C 364 |
Chain | Residue |
C | GLU105 |
C | GLU143 |
C | HIS146 |
C | GLU229 |
C | AZI2366 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE C 365 |
Chain | Residue |
C | TRP139 |
C | GLU143 |
C | GLU196 |
C | GLU229 |
C | HIS232 |
C | AZI2366 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AZI C 2366 |
Chain | Residue |
C | GLU105 |
C | GLU143 |
C | GLU196 |
C | THR199 |
C | GLU229 |
C | FE364 |
C | FE365 |
C | HOH2442 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE D 364 |
Chain | Residue |
D | GLU105 |
D | GLU143 |
D | HIS146 |
D | GLU229 |
D | AZI3366 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE D 365 |
Chain | Residue |
D | GLU143 |
D | GLU196 |
D | GLU229 |
D | HIS232 |
D | AZI3366 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE AZI D 3366 |
Chain | Residue |
D | GLU105 |
D | GLU143 |
D | GLU196 |
D | THR199 |
D | FE364 |
D | FE365 |
D | HOH3442 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE E 364 |
Chain | Residue |
E | GLU105 |
E | GLU143 |
E | HIS146 |
E | GLU229 |
E | AZI4366 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE E 365 |
Chain | Residue |
E | TRP139 |
E | GLU143 |
E | GLU196 |
E | GLU229 |
E | HIS232 |
E | AZI4366 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AZI E 4366 |
Chain | Residue |
E | GLU105 |
E | GLU143 |
E | GLU196 |
E | THR199 |
E | GLU229 |
E | FE364 |
E | FE365 |
E | HOH4442 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE F 364 |
Chain | Residue |
F | GLU105 |
F | GLU143 |
F | HIS146 |
F | GLU229 |
F | AZI5366 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE F 365 |
Chain | Residue |
F | GLU143 |
F | GLU196 |
F | GLU229 |
F | HIS232 |
F | AZI5366 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE AZI F 5366 |
Chain | Residue |
F | GLU105 |
F | GLU143 |
F | GLU196 |
F | THR199 |
F | GLU229 |
F | FE364 |
F | FE365 |
F | HOH5442 |
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 |