3U6W
Truncated M. tuberculosis LeuA (1-425) complexed with KIV
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 | 4 |
Details | BINDING SITE FOR RESIDUE MN A 426 |
Chain | Residue |
A | ASP81 |
A | HIS285 |
A | HIS287 |
A | KIV427 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN B 426 |
Chain | Residue |
B | ASP81 |
B | HIS285 |
B | HIS287 |
B | KIV427 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KIV A 427 |
Chain | Residue |
A | ASP81 |
A | LEU143 |
A | SER216 |
A | GLU218 |
A | PRO252 |
A | THR254 |
A | HIS285 |
A | HIS287 |
A | MN426 |
A | ARG80 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE KIV B 427 |
Chain | Residue |
B | ARG80 |
B | ASP81 |
B | GLU218 |
B | PRO252 |
B | THR254 |
B | HIS285 |
B | HIS287 |
B | MN426 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 428 |
Chain | Residue |
A | PHE313 |
A | ASN315 |
A | VAL352 |
A | ASN356 |
A | LEU358 |
A | PRO359 |
B | HIS361 |
B | ARG363 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 428 |
Chain | Residue |
A | HIS361 |
A | ARG363 |
B | PHE313 |
B | ASN315 |
B | VAL352 |
B | ASN356 |
B | LEU358 |
B | PRO359 |
B | VAL360 |
B | HOH438 |
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 |