1GXS
Crystal Structure of Hydroxynitrile Lyase from Sorghum bicolor in Complex with Inhibitor Benzoic Acid: a novel cyanogenic enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004185 | molecular_function | serine-type carboxypeptidase activity |
| D | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00560 |
| Number of Residues | 18 |
| Details | CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. LtyVtVrGAGHlVPvhrP |
| Chain | Residue | Details |
| B | LEU404-PRO421 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"12356304","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GXS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P08819","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12356304","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GXS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P08819","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12356304 |
| Chain | Residue | Details |
| A | SER158 | |
| A | TRP270 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 12356304 |
| Chain | Residue | Details |
| C | SER158 | |
| C | TRP270 |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 382 |
| Chain | Residue | Details |
| A | SER158 | electrostatic stabiliser, modifies pKa |
| A | TRP270 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 382 |
| Chain | Residue | Details |
| C | SER158 | electrostatic stabiliser, modifies pKa |
| C | TRP270 | proton shuttle (general acid/base) |
