6ISP
structure of Candida antarctica Lipase B mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triacylglycerol lipase activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004806 | molecular_function | triacylglycerol lipase activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004806 | molecular_function | triacylglycerol lipase activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016042 | biological_process | lipid catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CPQ D 401 |
| Chain | Residue |
| A | CPQ403 |
| D | THR186 |
| D | ASN196 |
| D | PRO218 |
| D | PHE220 |
| D | CPQ402 |
| D | HOH501 |
| D | HOH535 |
| D | HOH597 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CPQ D 402 |
| Chain | Residue |
| A | PRO218 |
| D | ALA287 |
| D | CPQ401 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | ASP223 |
| A | HOH668 |
| A | HOH699 |
| D | ASP223 |
| D | HOH651 |
| D | HOH691 |
| D | HOH698 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue CPQ A 402 |
| Chain | Residue |
| A | THR186 |
| A | VAL194 |
| A | SER195 |
| A | ASN196 |
| A | SER197 |
| A | LEU199 |
| A | GLN213 |
| A | PRO218 |
| A | PHE220 |
| A | CPQ404 |
| A | CPQ405 |
| A | HOH519 |
| A | HOH579 |
| A | HOH665 |
| A | HOH671 |
| C | ARG302 |
| C | THR316 |
| C | PRO317 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue CPQ A 403 |
| Chain | Residue |
| A | PRO143 |
| A | TYR282 |
| A | HOH531 |
| A | HOH602 |
| A | HOH638 |
| D | LEU140 |
| D | ALA185 |
| D | GLN191 |
| D | CPQ401 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue CPQ A 404 |
| Chain | Residue |
| A | VAL139 |
| A | LEU140 |
| A | ALA185 |
| A | THR186 |
| A | GLN191 |
| A | CPQ402 |
| A | HOH561 |
| D | LEU144 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue CPQ A 405 |
| Chain | Residue |
| A | GLN46 |
| A | PHE71 |
| A | ALA283 |
| A | ALA284 |
| A | ALA287 |
| A | CPQ402 |
| C | PRO317 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CPQ C 401 |
| Chain | Residue |
| B | CPQ402 |
| C | CPQ402 |
| C | CPQ403 |
| C | HOH633 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue CPQ C 402 |
| Chain | Residue |
| B | CPQ402 |
| C | THR186 |
| C | VAL194 |
| C | GLN213 |
| C | PRO218 |
| C | PHE220 |
| C | CPQ401 |
| C | HOH517 |
| C | HOH622 |
| C | HOH633 |
| C | HOH816 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue CPQ C 403 |
| Chain | Residue |
| C | GLN46 |
| C | PHE71 |
| C | ALA283 |
| C | ALA287 |
| C | CPQ401 |
| C | HOH506 |
| C | HOH514 |
| C | HOH633 |
| C | HOH801 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| B | ASP223 |
| B | HOH674 |
| B | HOH704 |
| B | HOH706 |
| C | ASP223 |
| C | HOH646 |
| C | HOH673 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue CPQ B 402 |
| Chain | Residue |
| C | CPQ401 |
| C | CPQ402 |
| B | THR186 |
| B | VAL194 |
| B | GLN213 |
| B | PRO218 |
| B | PHE220 |
| B | HOH562 |
| B | HOH651 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CPQ B 403 |
| Chain | Residue |
| B | ALA185 |
| B | THR186 |
| B | HOH559 |
| C | PRO143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8087556","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






