4K6K
Crystal structure of CALB mutant D223G from Candida antarctica
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 401 |
| Chain | Residue |
| A | ALA18 |
| A | EDO402 |
| A | EDO404 |
| A | HOH577 |
| A | HOH626 |
| B | EDO401 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | EDO401 |
| A | EDO407 |
| A | EDO408 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | TYR203 |
| A | GLY207 |
| A | LYS208 |
| A | ASN209 |
| A | HOH578 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | TYR203 |
| A | PHE205 |
| A | EDO401 |
| A | HOH554 |
| B | THR316 |
| B | EDO401 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | TYR91 |
| A | ASN96 |
| A | EDO408 |
| A | HOH635 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 406 |
| Chain | Residue |
| A | EDO408 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 407 |
| Chain | Residue |
| A | ALA18 |
| A | EDO402 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 408 |
| Chain | Residue |
| A | EDO402 |
| A | EDO405 |
| A | EDO406 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 401 |
| Chain | Residue |
| A | EDO401 |
| A | EDO404 |
| A | HOH589 |
| B | PRO317 |
| B | LEU318 |
| B | HOH561 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"8527460","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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 |
