2XZ1
The Structure of the 2:2 (Fully 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 | 0000036 | molecular_function | acyl carrier activity |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0031177 | molecular_function | phosphopantetheine 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 | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 401 |
| Chain | Residue |
| A | GLU105 |
| A | GLU143 |
| A | HIS146 |
| A | GLU229 |
| A | FE402 |
| A | CAC501 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 402 |
| Chain | Residue |
| A | FE401 |
| A | CAC501 |
| A | GLU143 |
| A | GLU196 |
| A | GLU229 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 403 |
| Chain | Residue |
| A | GLU106 |
| A | ASN144 |
| A | ASP148 |
| B | CA403 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAC A 501 |
| Chain | Residue |
| A | GLU105 |
| A | TYR111 |
| A | GLU143 |
| A | GLU196 |
| A | THR199 |
| A | GLU229 |
| A | FE401 |
| A | FE402 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 401 |
| Chain | Residue |
| B | GLU105 |
| B | GLU143 |
| B | HIS146 |
| B | GLU229 |
| B | FE402 |
| B | CAC501 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 402 |
| Chain | Residue |
| B | GLU143 |
| B | GLU196 |
| B | GLU229 |
| B | FE401 |
| B | CAC501 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 403 |
| Chain | Residue |
| A | CA403 |
| B | GLU106 |
| B | ASN144 |
| B | ASP148 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CAC B 501 |
| Chain | Residue |
| B | GLU105 |
| B | TYR111 |
| B | GLU143 |
| B | GLU229 |
| B | FE401 |
| B | FE402 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PNY C 1138 |
| Chain | Residue |
| C | SEP38 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. KLGADSLDTVEIVMNL |
| Chain | Residue | Details |
| C | 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 | 12 |
| 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 | 2 |
| 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 |
