3IVU
Homocitrate Synthase Lys4 bound to 2-OG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004410 | molecular_function | homocitrate synthase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0004410 | molecular_function | homocitrate synthase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| 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 CO A 500 |
| Chain | Residue |
| A | GLU44 |
| A | HIS224 |
| A | HIS226 |
| A | HOH465 |
| A | AKG1000 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 503 |
| Chain | Residue |
| A | VAL217 |
| A | VAL217 |
| A | ARG214 |
| A | ARG214 |
| A | GLY215 |
| A | GLY215 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AKG A 1000 |
| Chain | Residue |
| A | ARG43 |
| A | GLU44 |
| A | HIS103 |
| A | ARG163 |
| A | SER165 |
| A | ALA195 |
| A | THR197 |
| A | HIS224 |
| A | HIS226 |
| A | HOH452 |
| A | HOH465 |
| A | CO500 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 500 |
| Chain | Residue |
| B | GLU44 |
| B | HIS224 |
| B | HIS226 |
| B | HOH422 |
| B | AKG1000 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 503 |
| Chain | Residue |
| B | ARG214 |
| B | ARG214 |
| B | GLY215 |
| B | GLY215 |
| B | VAL217 |
| B | VAL217 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG B 1000 |
| Chain | Residue |
| B | ARG43 |
| B | GLU44 |
| B | HIS103 |
| B | VAL125 |
| B | ARG163 |
| B | ALA195 |
| B | THR197 |
| B | HIS224 |
| B | HIS226 |
| B | HOH422 |
| B | HOH461 |
| B | HOH466 |
| B | CO500 |
Functional Information from PROSITE/UniProt
| site_id | PS00815 |
| Number of Residues | 17 |
| Details | AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LREGeQfanaFfdtekK |
| Chain | Residue | Details |
| A | LEU42-LYS58 |
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. IecHfHNDtGmAiA |
| Chain | Residue | Details |
| A | ILE221-ALA234 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O87198 |
| Chain | Residue | Details |
| A | HIS321 | |
| B | HIS321 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3IVU |
| Chain | Residue | Details |
| A | ARG43 | |
| A | HIS103 | |
| A | ARG163 | |
| B | ARG43 | |
| B | HIS103 | |
| B | ARG163 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT, ECO:0007744|PDB:3MI3 |
| Chain | Residue | Details |
| A | GLU44 | |
| A | HIS224 | |
| A | HIS226 | |
| B | GLU44 | |
| B | HIS224 | |
| B | HIS226 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20089861, ECO:0007744|PDB:3MI3 |
| Chain | Residue | Details |
| A | ASP123 | |
| A | THR197 | |
| B | ASP123 | |
| B | THR197 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19776021, ECO:0007744|PDB:3IVT |
| Chain | Residue | Details |
| A | SER165 | |
| B | SER165 |
