2FTP
Crystal Structure of hydroxymethylglutaryl-CoA lyase from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004419 | molecular_function | hydroxymethylglutaryl-CoA lyase activity |
| A | 0006552 | biological_process | L-leucine catabolic process |
| A | 0008300 | biological_process | isoprenoid catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0046247 | biological_process | terpene catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046951 | biological_process | ketone body biosynthetic process |
| A | 0047445 | molecular_function | 3-hydroxy-3-isohexenylglutaryl-CoA lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 3000 |
| Chain | Residue |
| A | ASP16 |
| A | HIS207 |
| A | HIS209 |
| A | ASN249 |
| A | HOH3187 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 2000 |
| Chain | Residue |
| A | MET59 |
| A | ALA60 |
| A | GLY61 |
| A | SER62 |
| A | ALA63 |
| A | ASN114 |
| A | HOH3167 |
| A | SER49 |
| A | PHE50 |
| A | VAL51 |
| A | PRO53 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | LYS54 |
| A | PHE101 |
| A | ALA102 |
| A | ALA103 |
| A | ASN112 |
| A | ILE113 |
| A | SER143 |
| A | HOH3037 |
Functional Information from PROSITE/UniProt
| site_id | PS01062 |
| Number of Residues | 10 |
| Details | HMG_COA_LYASE Hydroxymethylglutaryl-coenzyme A lyase active site. SVAGLGGCPY |
| Chain | Residue | Details |
| A | SER233-TYR242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 267 |
| 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 | 1 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10115","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal Structure of hydroxymethylglutaryl-CoA lyase from Pseudomonas aeruginosa.","authors":["Xiao T.","Evdokimova E.","Liu Y.","Kudritska M.","Savchenko A.","Pai E.F.","Edwards A."]}}]} |
| Chain | Residue | Details |
