5E9G
Structural insights of isocitrate lyases from Magnaporthe oryzae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004451 | molecular_function | isocitrate lyase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006097 | biological_process | glyoxylate cycle |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0009514 | cellular_component | glyoxysome |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0046421 | molecular_function | methylisocitrate lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004451 | molecular_function | isocitrate lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0006097 | biological_process | glyoxylate cycle |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0009514 | cellular_component | glyoxysome |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0046421 | molecular_function | methylisocitrate lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004451 | molecular_function | isocitrate lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005777 | cellular_component | peroxisome |
| C | 0006097 | biological_process | glyoxylate cycle |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0009514 | cellular_component | glyoxysome |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0046421 | molecular_function | methylisocitrate lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004451 | molecular_function | isocitrate lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005777 | cellular_component | peroxisome |
| D | 0006097 | biological_process | glyoxylate cycle |
| D | 0006099 | biological_process | tricarboxylic acid cycle |
| D | 0009514 | cellular_component | glyoxysome |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0046421 | molecular_function | methylisocitrate lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue GLV A 601 |
| Chain | Residue |
| A | TYR104 |
| A | MG603 |
| A | SER106 |
| A | GLY107 |
| A | TRP108 |
| A | ASP177 |
| A | HIS204 |
| A | ARG252 |
| A | TRP403 |
| A | THR467 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | TRP108 |
| A | CYS215 |
| A | GLY216 |
| A | HIS217 |
| A | ARG252 |
| A | GLU405 |
| A | ASN433 |
| A | SER435 |
| A | THR467 |
| A | HOH716 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | ASP177 |
| A | GLV601 |
| A | HOH701 |
| A | HOH716 |
| A | HOH717 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue GLV B 601 |
| Chain | Residue |
| B | TYR104 |
| B | SER106 |
| B | GLY107 |
| B | TRP108 |
| B | ASP177 |
| B | HIS204 |
| B | ARG252 |
| B | TRP403 |
| B | THR467 |
| B | GOL602 |
| B | MG603 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | CYS215 |
| B | GLY216 |
| B | HIS217 |
| B | ARG252 |
| B | GLU405 |
| B | ASN433 |
| B | SER435 |
| B | SER437 |
| B | THR467 |
| B | GLV601 |
| B | HOH704 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 603 |
| Chain | Residue |
| B | ASP177 |
| B | LYS213 |
| B | GLV601 |
| B | HOH702 |
| B | HOH704 |
| B | HOH705 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | binding site for residue GLV C 601 |
| Chain | Residue |
| C | TYR104 |
| C | SER106 |
| C | GLY107 |
| C | TRP108 |
| C | ASP177 |
| C | ARG252 |
| C | TRP403 |
| C | MG602 |
| C | HOH706 |
| C | HOH723 |
| C | HOH728 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 602 |
| Chain | Residue |
| C | ASP177 |
| C | GLV601 |
| C | HOH706 |
| C | HOH707 |
| C | HOH726 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GLV D 601 |
| Chain | Residue |
| D | TYR104 |
| D | SER106 |
| D | GLY107 |
| D | TRP108 |
| D | ASP177 |
| D | HIS204 |
| D | ARG252 |
| D | TRP403 |
| D | THR467 |
| D | GOL602 |
| D | MG603 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL D 602 |
| Chain | Residue |
| D | CYS215 |
| D | GLY216 |
| D | HIS217 |
| D | ARG252 |
| D | GLU405 |
| D | ASN433 |
| D | SER435 |
| D | SER437 |
| D | GLV601 |
| D | HOH703 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 603 |
| Chain | Residue |
| D | ASP177 |
| D | GLV601 |
| D | HOH703 |
| D | HOH709 |
| D | HOH710 |
Functional Information from PROSITE/UniProt
| site_id | PS00161 |
| Number of Residues | 6 |
| Details | ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHM |
| Chain | Residue | Details |
| A | LYS213-MET218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 |
| Chain | Residue | Details |
| A | CYS215 | |
| B | CYS215 | |
| C | CYS215 | |
| D | CYS215 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WKK7 |
| Chain | Residue | Details |
| A | SER106 | |
| B | ARG252 | |
| B | ASN433 | |
| B | THR467 | |
| C | SER106 | |
| C | ASP177 | |
| C | GLY216 | |
| C | ARG252 | |
| C | ASN433 | |
| C | THR467 | |
| D | SER106 | |
| A | ASP177 | |
| D | ASP177 | |
| D | GLY216 | |
| D | ARG252 | |
| D | ASN433 | |
| D | THR467 | |
| A | GLY216 | |
| A | ARG252 | |
| A | ASN433 | |
| A | THR467 | |
| B | SER106 | |
| B | ASP177 | |
| B | GLY216 |
