3EI9
Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana complexed with L-Glu: 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 | 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 | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PL6 A 433 |
| Chain | Residue |
| A | TYR37 |
| A | ASN209 |
| A | ASP237 |
| A | TYR240 |
| A | SER267 |
| A | SER269 |
| A | ARG278 |
| A | ARG404 |
| B | TYR94 |
| B | ASN309 |
| A | PHE39 |
| A | ILE63 |
| A | GLY64 |
| A | GLY127 |
| A | ALA128 |
| A | LYS129 |
| A | TYR152 |
| A | CYS205 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 434 |
| Chain | Residue |
| A | LYS81 |
| A | SER92 |
| A | ASN313 |
| A | HOH549 |
| A | HOH648 |
| A | HOH954 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 435 |
| Chain | Residue |
| A | PHE111 |
| A | TYR112 |
| A | SER238 |
| A | ARG250 |
| A | SER251 |
| A | GLU264 |
| A | ALA266 |
| A | TYR271 |
| A | TRP281 |
| A | HOH486 |
| A | HOH692 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 436 |
| Chain | Residue |
| A | LYS109 |
| A | THR110 |
| A | PHE111 |
| A | TYR112 |
| A | GLY113 |
| A | LEU115 |
| A | HOH485 |
| A | HOH589 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 437 |
| Chain | Residue |
| A | HIS429 |
| A | HIS430 |
| A | HOH870 |
| A | HOH879 |
| B | GLY176 |
| B | ASN177 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 438 |
| Chain | Residue |
| A | LYS101 |
| A | ARG104 |
| A | ASP119 |
| A | ASP120 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PL6 B 433 |
| Chain | Residue |
| A | TYR94 |
| A | ASN309 |
| 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 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 434 |
| Chain | Residue |
| B | LYS81 |
| B | SER92 |
| B | ASN313 |
| B | HOH878 |
| B | HOH1014 |
| B | HOH1155 |
| B | HOH1280 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 435 |
| Chain | Residue |
| B | PHE111 |
| B | TYR112 |
| B | SER238 |
| B | ARG250 |
| B | SER251 |
| B | GLU264 |
| B | ALA266 |
| B | TYR271 |
| B | TRP281 |
| B | HOH823 |
| B | HOH953 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 436 |
| Chain | Residue |
| A | HOH485 |
| B | PHE111 |
| B | GLY113 |
| B | LEU115 |
| B | HOH790 |
| B | HOH942 |
| B | HOH1223 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 437 |
| Chain | Residue |
| B | ASP119 |
| B | ASP120 |
| B | LYS101 |
| B | ARG104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18952095 |
| Chain | Residue | Details |
| A | TYR37 | |
| B | TYR37 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095 |
| Chain | Residue | Details |
| A | GLY64 | |
| A | ASN309 | |
| A | ARG404 | |
| B | GLY64 | |
| B | TYR94 | |
| B | ALA128 | |
| B | LYS129 | |
| B | TYR152 | |
| B | ASN209 | |
| B | TYR240 | |
| B | SER267 | |
| A | TYR94 | |
| B | ARG278 | |
| B | ASN309 | |
| B | ARG404 | |
| A | ALA128 | |
| A | LYS129 | |
| A | TYR152 | |
| A | ASN209 | |
| A | TYR240 | |
| A | SER267 | |
| A | ARG278 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:18952095, ECO:0000305|PubMed:17583737 |
| Chain | Residue | Details |
| A | ASN270 | |
| B | ASN270 |
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 |
