3EIB
Crystal structure of K270N variant of LL-diaminopimelate aminotransferase from Arabidopsis thaliana
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 | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 433 |
| Chain | Residue |
| A | GLY127 |
| A | SER269 |
| A | ASN270 |
| A | ARG278 |
| A | SO4434 |
| A | HOH777 |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 434 |
| Chain | Residue |
| A | PHE39 |
| A | ILE63 |
| A | GLY64 |
| A | TYR152 |
| A | ASN209 |
| A | TYR240 |
| A | ARG404 |
| A | PLP433 |
| A | HOH437 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 435 |
| Chain | Residue |
| A | LYS101 |
| A | ARG104 |
| A | ASP119 |
| A | ASP120 |
| A | HOH841 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 436 |
| Chain | Residue |
| A | LYS81 |
| A | ASN313 |
| A | GLN316 |
| A | HOH555 |
| A | HOH715 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 433 |
| Chain | Residue |
| A | TYR94 |
| A | ASN309 |
| B | GLY127 |
| B | ALA128 |
| B | LYS129 |
| B | TYR152 |
| B | ASN209 |
| B | ASP237 |
| B | TYR240 |
| B | SER267 |
| B | SER269 |
| B | ASN270 |
| B | ARG278 |
| B | SO4434 |
| B | HOH1036 |
| B | HOH1103 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 434 |
| Chain | Residue |
| B | PHE39 |
| B | ILE63 |
| B | GLY64 |
| B | TYR152 |
| B | ASN209 |
| B | TYR240 |
| B | ARG404 |
| B | PLP433 |
| B | HOH961 |
| B | HOH1093 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 435 |
| Chain | Residue |
| B | LYS101 |
| B | ARG104 |
| B | ASP119 |
| B | ASP120 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 436 |
| Chain | Residue |
| A | HIS429 |
| A | HIS430 |
| B | GLY176 |
| B | ASN177 |
| B | HOH936 |
| B | HOH1230 |
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 |
