6E1J
Crystal Structure of Methylthioalkylmalate Synthase (BjuMAM1.1) from Brassica juncea
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0043436 | biological_process | oxoacid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0043436 | biological_process | oxoacid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 601 |
| Chain | Residue |
| A | ASP90 |
| A | HIS288 |
| A | HIS290 |
| A | KMT603 |
| A | HOH739 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 602 |
| Chain | Residue |
| A | VAL145 |
| A | GLU147 |
| A | HOH757 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue KMT A 603 |
| Chain | Residue |
| A | ASP90 |
| A | VAL182 |
| A | GLU223 |
| A | GLU227 |
| A | ALA253 |
| A | PRO255 |
| A | THR257 |
| A | HIS288 |
| A | HIS290 |
| A | MN601 |
| A | HOH732 |
| A | ARG89 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue COA A 604 |
| Chain | Residue |
| A | GLY386 |
| A | ILE387 |
| A | ASP390 |
| A | LYS394 |
| A | LEU422 |
| A | ARG425 |
| A | HIS426 |
| A | ARG452 |
| A | HOH714 |
| A | HOH722 |
| A | HOH742 |
| A | HOH824 |
| A | HOH851 |
| B | ARG89 |
| B | GLN93 |
| B | PHE123 |
| B | SER126 |
| B | ARG160 |
| B | SER161 |
| B | PHE184 |
| B | THR185 |
| B | LYS195 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 601 |
| Chain | Residue |
| B | ASP90 |
| B | HIS288 |
| B | HIS290 |
| B | KMT602 |
| B | HOH753 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue KMT B 602 |
| Chain | Residue |
| B | ARG89 |
| B | ASP90 |
| B | GLU227 |
| B | PRO255 |
| B | THR257 |
| B | HIS288 |
| B | HIS290 |
| B | MN601 |
| B | HOH753 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue COA B 603 |
| Chain | Residue |
| A | GLN93 |
| A | PHE123 |
| A | SER126 |
| A | ARG160 |
| A | SER161 |
| A | PHE184 |
| A | THR185 |
| A | LYS195 |
| A | HOH728 |
| A | HOH820 |
| B | SER385 |
| B | GLY386 |
| B | ILE387 |
| B | ASP390 |
| B | LYS394 |
| B | LEU422 |
| B | GLY424 |
| B | ARG425 |
| B | HIS426 |
| B | ARG452 |
| B | HOH705 |
| B | HOH794 |
Functional Information from PROSITE/UniProt
| site_id | PS00815 |
| Number of Residues | 17 |
| Details | AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGeQspgaAltppqK |
| Chain | Residue | Details |
| A | LEU88-LYS104 |
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. FsaHcHNDlGvAtA |
| Chain | Residue | Details |
| A | PHE285-ALA298 |
