3EI8
Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with LL-DAP: External aldimine form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0009862 | biological_process | systemic acquired resistance, salicylic acid mediated signaling pathway |
| A | 0010285 | molecular_function | L,L-diaminopimelate aminotransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0009862 | biological_process | systemic acquired resistance, salicylic acid mediated signaling pathway |
| B | 0010285 | molecular_function | L,L-diaminopimelate aminotransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 433 |
| Chain | Residue |
| A | GLY127 |
| A | SER269 |
| A | ARG278 |
| A | HOH679 |
| B | TYR94 |
| B | ASN309 |
| A | ALA128 |
| A | LYS129 |
| A | TYR152 |
| A | CYS205 |
| A | ASN209 |
| A | ASP237 |
| A | TYR240 |
| A | SER267 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 434 |
| Chain | Residue |
| A | LYS101 |
| A | ARG104 |
| A | ASP119 |
| A | ASP120 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 435 |
| Chain | Residue |
| A | LYS81 |
| A | SER92 |
| A | ASN313 |
| A | HOH547 |
| A | HOH624 |
| A | HOH766 |
| A | HOH903 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 436 |
| Chain | Residue |
| A | PHE111 |
| A | SER238 |
| A | MET242 |
| A | ARG250 |
| A | SER251 |
| A | GLU264 |
| A | ALA266 |
| A | TYR271 |
| A | TRP281 |
| A | HOH484 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 437 |
| Chain | Residue |
| A | PHE111 |
| A | GLY113 |
| A | LEU115 |
| A | GLU254 |
| A | HOH504 |
| A | HOH945 |
| B | THR110 |
| B | HOH790 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PL5 B 433 |
| Chain | Residue |
| A | TYR94 |
| A | ASN309 |
| A | HOH486 |
| B | TYR37 |
| B | PHE39 |
| B | ILE63 |
| B | GLY64 |
| B | GLY127 |
| B | ALA128 |
| B | LYS129 |
| B | TYR152 |
| B | TYR155 |
| B | CYS205 |
| B | ASN209 |
| B | ASP237 |
| B | TYR240 |
| B | SER267 |
| B | SER269 |
| B | ARG278 |
| B | ARG404 |
| B | HOH926 |
| B | HOH1089 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 434 |
| Chain | Residue |
| B | LYS101 |
| B | ARG104 |
| B | ASP120 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 435 |
| Chain | Residue |
| B | LYS81 |
| B | SER92 |
| B | ASN313 |
| B | GLN316 |
| B | HOH854 |
| B | HOH996 |
| B | HOH1145 |
| B | HOH1200 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL B 436 |
| Chain | Residue |
| B | PHE111 |
| B | SER238 |
| B | MET242 |
| B | ARG250 |
| B | SER251 |
| B | GLU264 |
| B | ALA266 |
| B | TYR271 |
| B | TRP281 |
| B | HOH786 |
| B | HOH929 |
| B | HOH1104 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 437 |
| Chain | Residue |
| A | THR110 |
| B | TYR112 |
| B | GLY113 |
| B | HOH790 |
| B | HOH901 |
| B | HOH1081 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18952095","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17583737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18952095","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"18952095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17583737","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cs1 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | ASP237 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cs1 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | ASP237 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cs1 |
| Chain | Residue | Details |
| A | GLY93 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cs1 |
| Chain | Residue | Details |
| B | GLY93 |
