2RF8
Crystal Structure of the mutant C2A conjugated bile acid hydrolase from Clostridium perfringens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006699 | biological_process | bile acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0045302 | molecular_function | choloylglycine hydrolase activity |
| A | 0047742 | molecular_function | chenodeoxycholoyltaurine hydrolase activity |
| A | 7770003 | molecular_function | amino acid conjugated cholate hydrolase activity |
| A | 7770006 | molecular_function | L-phenylalanine conjugated cholate hydrolase activity |
| A | 7770007 | molecular_function | L-arginine conjugated cholate hydrolase activity |
| A | 7770008 | molecular_function | L-histidine conjugated cholate hydrolase activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006699 | biological_process | bile acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0045302 | molecular_function | choloylglycine hydrolase activity |
| B | 0047742 | molecular_function | chenodeoxycholoyltaurine hydrolase activity |
| B | 7770003 | molecular_function | amino acid conjugated cholate hydrolase activity |
| B | 7770006 | molecular_function | L-phenylalanine conjugated cholate hydrolase activity |
| B | 7770007 | molecular_function | L-arginine conjugated cholate hydrolase activity |
| B | 7770008 | molecular_function | L-histidine conjugated cholate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 332 |
| Chain | Residue |
| A | ALA2 |
| A | ASN82 |
| A | PRO84 |
| A | ASN175 |
| A | ARG228 |
| A | MET261 |
| B | GLN212 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 333 |
| Chain | Residue |
| B | MET1 |
| B | ASN82 |
| B | PRO84 |
| B | ASN175 |
| B | PRO225 |
| B | HOH373 |
| B | HOH379 |
| A | LEU210 |
| A | GLY211 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 334 |
| Chain | Residue |
| A | ASN36 |
| A | LYS38 |
| A | ASN312 |
| A | HOH419 |
Functional Information from PROSITE/UniProt
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLnFPV |
| Chain | Residue | Details |
| A | ALA79-VAL85 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile; acyl-thioester intermediate","evidences":[{"source":"PubMed","id":"15823032","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"38326608","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15823032","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BJF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
