6J1R
Crystal structure of Candida Antarctica Lipase B mutant - RR
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 | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | LYS208 |
| B | ARG249 |
| B | SER250 |
| B | HOH523 |
| B | HOH525 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ASP49 |
| B | GLN270 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | SER26 |
| B | PRO27 |
| B | HOH645 |
| A | SER123 |
| A | HOH523 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | THR40 |
| B | SER105 |
| B | GLN106 |
| B | LEU157 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 405 |
| Chain | Residue |
| A | GLY142 |
| B | VAL215 |
| B | GLY217 |
| B | HOH653 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LYS208 |
| A | ARG249 |
| A | SER250 |
| A | HOH545 |
| A | HOH565 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | THR165 |
| A | ARG168 |
| A | LYS308 |
| A | HOH535 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | THR40 |
| A | SER105 |
| A | GLN106 |
| A | ASP134 |
| A | LEU157 |
| A | HIS224 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LYS32 |
| B | PRO12 |
| B | LYS13 |
| B | HOH624 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | VAL286 |
| A | LYS290 |
| B | VAL221 |
| B | PRO260 |
| B | LEU261 |
| B | HOH614 |
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 |
