5GZZ
Crystal Structure of FIN219-SjGST complex with JA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
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 |
B | TYR7 | |
D | TRP41 | |
D | ASN54 | |
D | GLN67 | |
E | TYR7 | |
E | TRP41 | |
E | ASN54 | |
E | GLN67 | |
F | TYR7 | |
F | TRP41 | |
F | ASN54 | |
B | TRP41 | |
F | GLN67 | |
G | TYR7 | |
G | TRP41 | |
G | ASN54 | |
G | GLN67 | |
B | ASN54 | |
B | GLN67 | |
C | TYR7 | |
C | TRP41 | |
C | ASN54 | |
C | GLN67 | |
D | TYR7 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
B | TYR111 | |
C | TYR111 | |
D | TYR111 | |
E | TYR111 | |
F | TYR111 | |
G | 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 |