6KTQ
Crystal structure of catalytic domain of homocitrate synthase from Sulfolobus acidocaldarius (SaHCS(dRAM)) in complex with alpha-ketoglutarate/Zn2+/CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004410 | molecular_function | homocitrate synthase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| 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 | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PROSITE/UniProt
| site_id | PS00816 |
| Number of Residues | 14 |
| Details | AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. FdiHaHNDlGmAvA |
| Chain | Residue | Details |
| A | PHE202-ALA215 |
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 | HIS299 | |
| B | HIS299 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O87198 |
| Chain | Residue | Details |
| A | ARG19 | |
| B | HIS83 | |
| B | ARG143 | |
| B | THR177 | |
| B | HIS205 | |
| B | HIS207 | |
| A | GLU20 | |
| A | HIS83 | |
| A | ARG143 | |
| A | THR177 | |
| A | HIS205 | |
| A | HIS207 | |
| B | ARG19 | |
| B | GLU20 |
