3HPS
Crystal structure of Mycobacterium tuberculosis LeuA complexed with ketoisocaproate (KIC)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| A | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003852 | molecular_function | 2-isopropylmalate synthase activity |
| B | 0003985 | molecular_function | acetyl-CoA C-acetyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030955 | molecular_function | potassium ion binding |
| 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 | 12 |
| Details | BINDING SITE FOR RESIDUE LEU A 703 |
| Chain | Residue |
| A | GLY562 |
| B | PRO534 |
| B | LEU535 |
| B | ALA536 |
| A | ASP563 |
| A | ASP564 |
| A | ALA565 |
| A | GLN566 |
| A | PRO625 |
| A | ILE627 |
| B | ASN532 |
| B | GLY533 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LEU B 703 |
| Chain | Residue |
| A | ASN532 |
| A | GLY533 |
| A | PRO534 |
| A | LEU535 |
| A | ALA536 |
| B | ASP563 |
| B | ASP564 |
| B | ALA565 |
| B | GLN566 |
| B | PRO625 |
| B | ILE627 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 701 |
| Chain | Residue |
| A | ASP81 |
| A | HIS285 |
| A | HIS287 |
| A | ASN321 |
| A | COI702 |
| A | HOH870 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COI A 702 |
| Chain | Residue |
| A | ARG80 |
| A | ASP81 |
| A | HIS167 |
| A | TYR169 |
| A | SER216 |
| A | GLU218 |
| A | ASN250 |
| A | PRO252 |
| A | THR254 |
| A | HIS285 |
| A | HIS287 |
| A | ZN701 |
| A | HOH870 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | PHE313 |
| A | ASN315 |
| A | ASN356 |
| A | LEU358 |
| A | PRO359 |
| A | HOH751 |
| A | HOH1196 |
| B | HIS361 |
| B | ARG363 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 701 |
| Chain | Residue |
| B | ASP81 |
| B | HIS285 |
| B | HIS287 |
| B | ASN321 |
| B | COI702 |
| B | HOH1047 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COI B 702 |
| Chain | Residue |
| B | ARG80 |
| B | ASP81 |
| B | LEU143 |
| B | HIS167 |
| B | TYR169 |
| B | GLU218 |
| B | PRO252 |
| B | THR254 |
| B | HIS285 |
| B | HIS287 |
| B | HOH648 |
| B | ZN701 |
| B | HOH1047 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 704 |
| Chain | Residue |
| A | HIS361 |
| A | ARG363 |
| B | PHE313 |
| B | ASN315 |
| B | VAL352 |
| B | ASN356 |
| B | LEU358 |
| B | PRO359 |
| B | HOH785 |
| B | HOH804 |
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 | 548 |
| Details | Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"HAMAP-Rule","id":"MF_00572","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 317 |
| Details | Region: {"description":"N-terminal domain","evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 110 |
| Details | Region: {"description":"Subdomain I","evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SR9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3U6W","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00572","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1SR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FIG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HQ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3U6W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00572","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22352945","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3HPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HQ1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15159544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FIG","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
