6J1Q
Crystal structure of Candida Antarctica Lipase B mutant - RS
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 A 401 |
| Chain | Residue |
| A | LYS208 |
| A | ARG249 |
| A | SER250 |
| A | HOH531 |
| A | HOH536 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | HOH690 |
| B | SER123 |
| A | SER26 |
| A | PRO27 |
| A | HOH522 |
| A | HOH660 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | SER120 |
| A | LYS124 |
| A | EPE413 |
| A | HOH516 |
| A | HOH588 |
| A | HOH617 |
| A | HOH662 |
| B | THR245 |
| B | GLN247 |
| B | HOH537 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | TYR203 |
| A | PHE205 |
| A | ASN206 |
| A | HOH525 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | THR21 |
| A | PRO45 |
| A | TRP65 |
| A | SER67 |
| A | EDO407 |
| A | HOH544 |
| A | HOH582 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ARG242 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | THR43 |
| A | PRO45 |
| A | GLN46 |
| A | EDO405 |
| A | HOH653 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | EDO409 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | THR40 |
| A | SER105 |
| A | GLN106 |
| A | GLN157 |
| A | VAL189 |
| A | EDO408 |
| A | HOH549 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | GLN231 |
| A | TYR234 |
| A | ARG238 |
| A | ASP265 |
| A | EPE412 |
| A | HOH501 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | ALA8 |
| A | PRO299 |
| A | TYR300 |
| A | HOH686 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue EPE A 412 |
| Chain | Residue |
| A | ARG238 |
| A | ASP252 |
| A | GLY254 |
| A | ILE255 |
| A | THR256 |
| A | ASP257 |
| A | EDO410 |
| A | HOH501 |
| A | HOH503 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue EPE A 413 |
| Chain | Residue |
| A | GLY4 |
| A | PRO119 |
| A | SER120 |
| A | ARG122 |
| A | SO4403 |
| A | HOH532 |
| A | HOH562 |
| A | HOH622 |
| B | ALA25 |
| B | SER26 |
| B | SO4401 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 414 |
| Chain | Residue |
| A | CYS258 |
| B | LEU147 |
| B | VAL149 |
| B | HOH633 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 415 |
| Chain | Residue |
| A | ALA214 |
| A | VAL215 |
| A | GLY217 |
| A | HOH665 |
| B | GLY142 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | EPE413 |
| B | LYS208 |
| B | ARG249 |
| B | SER250 |
| B | HOH537 |
| B | HOH588 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | THR165 |
| B | ARG168 |
| B | LYS308 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | PRO7 |
| B | ALA8 |
| B | PRO299 |
| B | TYR300 |
| B | HOH505 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | ASN169 |
| B | PHE304 |
| B | HOH514 |
| B | HOH709 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| A | GLU188 |
| A | HOH715 |
| B | ALA283 |
| B | HOH557 |
| B | HOH626 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 406 |
| Chain | Residue |
| B | ALA287 |
| B | GLY288 |
| B | PRO289 |
| B | HOH515 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 407 |
| Chain | Residue |
| A | HOH736 |
| B | THR138 |
| B | VAL154 |
| B | HOH512 |
| B | HOH621 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 408 |
| Chain | Residue |
| B | PRO45 |
| B | SER67 |
| B | HOH698 |
| B | HOH781 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue 1PE B 409 |
| Chain | Residue |
| B | LEU144 |
| B | ASN292 |
| B | ARG309 |
| B | THR310 |
| B | CYS311 |
| B | GLY313 |
| B | HOH503 |
| B | HOH731 |
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 |
