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 | 510 |
| Details | Domain: {"description":"Pyruvate carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O87198","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O87198","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
