2ZTK
Crystal structure of homocitrate synthase from Thermus thermophilus complexed with homocitrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004410 | molecular_function | homocitrate synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0036440 | molecular_function | citrate synthase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HCA A 383 |
| Chain | Residue |
| A | ARG12 |
| A | THR166 |
| A | HIS195 |
| A | HIS197 |
| A | HIS292 |
| A | CU384 |
| A | HOH435 |
| A | HOH547 |
| A | GLU13 |
| A | GLN16 |
| A | HIS72 |
| A | LEU94 |
| A | ARG133 |
| A | SER135 |
| A | GLU137 |
| A | ALA164 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 384 |
| Chain | Residue |
| A | GLU13 |
| A | HIS195 |
| A | HIS197 |
| A | HCA383 |
| A | HOH547 |
Functional Information from PROSITE/UniProt
| site_id | PS00815 |
| Number of Residues | 17 |
| Details | AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LREGeQfekaNfstqdK |
| Chain | Residue | Details |
| A | LEU11-LYS27 |
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. IefHgHNDtGcAiA |
| Chain | Residue | Details |
| A | ILE192-ALA205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19996101","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19996101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZYF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19996101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZYF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19996101","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3A9I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
