5GZZ
Crystal Structure of FIN219-SjGST complex with JA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002376 | biological_process | immune system process |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006952 | biological_process | defense response |
| A | 0009864 | biological_process | induced systemic resistance, jasmonic acid mediated signaling pathway |
| A | 0010046 | biological_process | response to mycotoxin |
| A | 0010224 | biological_process | response to UV-B |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| A | 0018117 | biological_process | protein adenylylation |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0045087 | biological_process | innate immune response |
| A | 0070728 | molecular_function | L-leucine binding |
| A | 0071365 | biological_process | cellular response to auxin stimulus |
| A | 0080123 | molecular_function | jasmonoyl-L-amino acid ligase activity |
| A | 2000030 | biological_process | regulation of response to red or far red light |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0004364 | molecular_function | glutathione transferase activity |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| D | 0004364 | molecular_function | glutathione transferase activity |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| E | 0004364 | molecular_function | glutathione transferase activity |
| E | 0006749 | biological_process | glutathione metabolic process |
| E | 0016740 | molecular_function | transferase activity |
| F | 0004364 | molecular_function | glutathione transferase activity |
| F | 0006749 | biological_process | glutathione metabolic process |
| F | 0016740 | molecular_function | transferase activity |
| G | 0004364 | molecular_function | glutathione transferase activity |
| G | 0006749 | biological_process | glutathione metabolic process |
| G | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue JAA A 601 |
| Chain | Residue |
| A | THR121 |
| A | GLU533 |
| A | PHE125 |
| A | THR166 |
| A | TYR170 |
| A | PHE220 |
| A | VAL222 |
| A | HIS328 |
| A | GLY331 |
| A | TRP336 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue GSH B 301 |
| Chain | Residue |
| B | TRP8 |
| B | LEU13 |
| B | TRP41 |
| B | ASN54 |
| B | LEU55 |
| B | GLN67 |
| B | SER68 |
| B | HOH416 |
| C | ASP101 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GSH C 301 |
| Chain | Residue |
| B | ASP101 |
| C | TRP8 |
| C | LEU13 |
| C | ASN54 |
| C | LEU55 |
| C | GLN67 |
| C | TYR104 |
| C | HOH410 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue GSH D 301 |
| Chain | Residue |
| D | LEU13 |
| D | LYS45 |
| D | ASN54 |
| D | LEU55 |
| D | PRO56 |
| D | GLN67 |
| D | SER68 |
| D | HOH410 |
| D | HOH447 |
| D | HOH490 |
| E | GLY97 |
| E | ASP101 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GSH E 301 |
| Chain | Residue |
| D | ASP101 |
| E | LEU13 |
| E | ASN54 |
| E | LEU55 |
| E | PRO56 |
| E | GLN67 |
| E | SER68 |
| E | HOH423 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue GSH F 301 |
| Chain | Residue |
| E | LYS194 |
| F | TRP41 |
| F | ASN54 |
| F | LEU55 |
| F | GLN67 |
| F | SER68 |
| F | TYR104 |
| F | HOH401 |
| F | HOH408 |
| F | HOH447 |
| G | ASP101 |
| G | TYR104 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GSH G 301 |
| Chain | Residue |
| G | LEU13 |
| G | TRP41 |
| G | ASN54 |
| G | LEU55 |
| G | GLN67 |
| G | SER68 |
| G | HOH418 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270 |
| Chain | Residue | Details |
| C | ASN54 | |
| C | GLN67 | |
| D | TYR7 | |
| D | TRP41 | |
| D | ASN54 | |
| D | GLN67 | |
| E | TYR7 | |
| E | TRP41 | |
| E | ASN54 | |
| E | GLN67 | |
| F | TYR7 | |
| F | TRP41 | |
| F | ASN54 | |
| F | GLN67 | |
| G | TYR7 | |
| G | TRP41 | |
| G | ASN54 | |
| G | GLN67 | |
| B | TYR7 | |
| B | TRP41 | |
| B | ASN54 | |
| B | GLN67 | |
| C | TYR7 | |
| C | TRP41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| G | TYR111 | |
| B | TYR111 | |
| C | TYR111 | |
| D | TYR111 | |
| E | TYR111 | |
| F | TYR111 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28223489, ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL, ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP |
| Chain | Residue | Details |
| A | THR166 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22628555, ECO:0000269|PubMed:28223489, ECO:0007744|PDB:4EPL, ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI, ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL, ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR, ECO:0007744|PDB:5GZZ |
| Chain | Residue | Details |
| A | HIS328 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28223489, ECO:0007744|PDB:5ECL, ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, ECO:0007744|PDB:5ECP, ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR |
| Chain | Residue | Details |
| A | LYS530 |
