2Z20
Crystal structure 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 | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 700 |
| Chain | Residue |
| A | PHE39 |
| A | HOH994 |
| A | ILE63 |
| A | GLY64 |
| A | TYR152 |
| A | ASN209 |
| A | TYR240 |
| A | ARG404 |
| A | PLP701 |
| A | HOH845 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 800 |
| Chain | Residue |
| B | PHE39 |
| B | ILE63 |
| B | GLY64 |
| B | TYR152 |
| B | ASN209 |
| B | TYR240 |
| B | LYS270 |
| B | ARG404 |
| B | PLP801 |
| B | HOH949 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 701 |
| Chain | Residue |
| A | GLY127 |
| A | ALA128 |
| A | LYS129 |
| A | ASN209 |
| A | ASP237 |
| A | TYR240 |
| A | SER267 |
| A | SER269 |
| A | LYS270 |
| A | ARG278 |
| A | SO4700 |
| B | TYR94 |
| B | ASN309 |
| B | HOH1046 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 801 |
| Chain | Residue |
| A | TYR94 |
| A | ASN309 |
| B | GLY127 |
| B | ALA128 |
| B | LYS129 |
| B | ASN209 |
| B | ASP237 |
| B | TYR240 |
| B | SER267 |
| B | SER269 |
| B | LYS270 |
| B | ARG278 |
| B | SO4800 |
| B | HOH939 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | LYS81 |
| A | SER92 |
| A | ASN313 |
| A | GLN316 |
| A | ALA317 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | ILE344 |
| A | THR348 |
| A | LYS422 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 802 |
| Chain | Residue |
| B | LYS81 |
| B | ASN313 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 803 |
| Chain | Residue |
| B | GLN423 |
| B | LYS426 |
| B | HIS427 |
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 | GLU72 | |
| B | GLU72 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095 |
| Chain | Residue | Details |
| A | GLY99 | |
| A | ILE344 | |
| A | ARG404 | |
| B | GLY99 | |
| B | LYS129 | |
| B | GLY163 | |
| B | GLN164 | |
| B | ASN187 | |
| B | MSE244 | |
| B | THR275 | |
| B | ARG302 | |
| A | LYS129 | |
| B | ASN313 | |
| B | ILE344 | |
| B | ARG404 | |
| A | GLY163 | |
| A | GLN164 | |
| A | ASN187 | |
| A | MSE244 | |
| A | THR275 | |
| A | ARG302 | |
| A | ASN313 |
| 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 | CYS305 | |
| B | CYS305 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | TYR152 | |
| A | ASP237 | |
| A | LYS270 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | TYR152 | |
| B | ASP237 | |
| B | LYS270 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP237 | |
| A | PHE139 | |
| A | LYS270 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP237 | |
| B | PHE139 | |
| B | LYS270 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP237 | |
| A | LYS270 | |
| A | PHE168 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP237 | |
| B | LYS270 | |
| B | PHE168 |
