6J1T
Crystal structure of Candida Antarctica Lipase B mutant SR with product analogue
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 | 7 |
| Details | binding site for residue B7U A 401 |
| Chain | Residue |
| A | THR40 |
| A | THR138 |
| A | VAL154 |
| A | GLN157 |
| A | ILE189 |
| A | LEU278 |
| A | ILE285 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | SER250 |
| A | HOH504 |
| A | HOH521 |
| A | LYS208 |
| A | ARG249 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | GLN11 |
| A | TYR82 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 404 |
| Chain | Residue |
| A | ASN169 |
| A | PRO303 |
| A | PHE304 |
| A | HOH569 |
| A | HOH602 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | LYS32 |
| A | PRO33 |
| A | SER94 |
| A | ASN97 |
| A | LYS98 |
| A | LEU99 |
| A | PRO100 |
| A | HOH524 |
| A | HOH634 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | TYR234 |
| A | ARG238 |
| A | ARG242 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | ASN206 |
| A | HOH556 |
| B | TYR91 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PEG A 409 |
| Chain | Residue |
| A | TYR91 |
| A | LYS98 |
| A | SER123 |
| A | HOH542 |
| B | SER26 |
| B | PRO27 |
| B | HOH581 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | LYS208 |
| B | ARG249 |
| B | SER250 |
| B | HOH506 |
| B | HOH533 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ARG242 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | ARG168 |
| B | LYS308 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue PGE B 404 |
| Chain | Residue |
| B | GLY288 |
| B | PRO289 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | THR21 |
| B | PRO45 |
| B | TRP65 |
| B | SER67 |
| B | EDO406 |
| B | HOH524 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | THR43 |
| B | GLN46 |
| B | EDO405 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | PRO299 |
| B | TYR300 |
| B | HOH570 |
| B | HOH609 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | GLN23 |
| B | ASP49 |
| B | ILE53 |
| B | HOH508 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | PRO12 |
| B | LYS13 |
| B | HOH631 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 410 |
| Chain | Residue |
| B | TYR203 |
| B | ASN206 |
| B | HOH596 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 411 |
| Chain | Residue |
| B | GLY24 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue PEG B 414 |
| Chain | Residue |
| B | ALA214 |
| B | VAL215 |
| B | GLY217 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue PEG B 415 |
| Chain | Residue |
| B | VAL235 |
| B | ARG238 |
| B | ASP252 |
| B | ASP257 |
| B | HOH507 |
| 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 |
