3HPX
Crystal structure of Mycobacterium tuberculosis LeuA active site domain 1-425 (truncation mutant delta:426-644)
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 | 0019752 | biological_process | carboxylic acid metabolic process |
| 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI A 701 |
| Chain | Residue |
| A | ASP81 |
| A | HIS285 |
| A | HIS287 |
| A | ASN321 |
| A | HOH434 |
| A | HOH612 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 702 |
| Chain | Residue |
| A | ASN356 |
| A | LEU358 |
| A | PRO359 |
| A | HOH491 |
| A | HOH602 |
| B | HIS361 |
| B | ARG363 |
| A | PHE313 |
| A | ASN315 |
| A | VAL352 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI B 701 |
| Chain | Residue |
| B | ASP81 |
| B | HIS285 |
| B | HIS287 |
| B | ASN321 |
| B | HOH427 |
| B | HOH610 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 703 |
| Chain | Residue |
| A | HIS361 |
| A | ARG363 |
| B | PHE313 |
| B | ASN315 |
| B | VAL352 |
| B | ASN356 |
| B | LEU358 |
| B | PRO359 |
| B | HOH477 |
| B | HOH605 |
Functional Information from PROSITE/UniProt
| site_id | PS00815 |
| Number of Residues | 17 |
| Details | AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LRDGnQalidPmsparK |
| Chain | Residue | Details |
| A | LEU79-LYS95 |
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. LslHpHNDrGtAvA |
| Chain | Residue | Details |
| A | LEU282-ALA295 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15159544, ECO:0000269|PubMed:22352945, ECO:0000312|PDB:1SR9, ECO:0000312|PDB:3U6W |
| Chain | Residue | Details |
| A | ARG80 | |
| A | THR254 | |
| B | ARG80 | |
| B | THR254 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:15159544, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:1SR9, ECO:0007744|PDB:3FIG, ECO:0007744|PDB:3HPS, ECO:0007744|PDB:3HPX, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1, ECO:0007744|PDB:3U6W |
| Chain | Residue | Details |
| A | ASP81 | |
| A | HIS285 | |
| A | HIS287 | |
| B | ASP81 | |
| B | HIS285 | |
| B | HIS287 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00572, ECO:0000305|PubMed:22352945, ECO:0007744|PDB:3HPZ, ECO:0007744|PDB:3HQ1 |
| Chain | Residue | Details |
| A | ASN321 | |
| B | ASN321 |
