6J1P
Crystal structure of Candida Antarctica Lipase B mutant - SR
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 | 4 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LYS208 |
| A | ARG249 |
| A | SER250 |
| A | HOH501 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | SER26 |
| A | PRO27 |
| A | HOH591 |
| B | SER123 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG168 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | ARG302 |
| A | ILE314 |
| A | VAL315 |
| A | THR316 |
| A | HOH569 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | VAL30 |
| A | GLY93 |
| A | HOH534 |
| A | HOH544 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | PRO299 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | THR43 |
| A | SER67 |
| A | PRO69 |
| A | PRO70 |
| A | PHE71 |
| A | HOH512 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | TYR203 |
| A | GLY207 |
| A | LYS208 |
| A | ASN209 |
| A | ACT413 |
| A | HOH503 |
| A | HOH592 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | PRO12 |
| A | LYS13 |
| A | SER14 |
| A | CL417 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ASP49 |
| A | TRP65 |
| A | HOH502 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | LEU144 |
| A | ALA148 |
| A | ASN292 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 412 |
| Chain | Residue |
| A | ALA214 |
| A | VAL215 |
| A | GLY217 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 413 |
| Chain | Residue |
| A | ASN206 |
| A | GLY207 |
| A | GLN247 |
| A | EDO408 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 414 |
| Chain | Residue |
| A | PRO45 |
| A | SER67 |
| A | HOH640 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 415 |
| Chain | Residue |
| A | GLU294 |
| A | ARG309 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 416 |
| Chain | Residue |
| A | ARG238 |
| A | HOH533 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 417 |
| Chain | Residue |
| A | PRO12 |
| A | LYS13 |
| A | EDO409 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 419 |
| Chain | Residue |
| A | GLY24 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | ASN206 |
| B | GLY207 |
| B | LYS208 |
| B | GLN247 |
| B | EDO406 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | LYS208 |
| B | ARG249 |
| B | SER250 |
| B | HOH503 |
| B | HOH582 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | ASN292 |
| B | CYS293 |
| B | GLU294 |
| B | ARG309 |
| B | THR310 |
| B | PGE417 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 404 |
| Chain | Residue |
| B | GLN11 |
| B | VAL15 |
| B | PRO69 |
| B | TYR82 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | ARG302 |
| B | THR310 |
| B | SER312 |
| B | GLY313 |
| B | ILE314 |
| B | VAL315 |
| B | HOH550 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| A | LYS124 |
| B | THR245 |
| B | GLN247 |
| B | ARG249 |
| B | SO4401 |
| B | HOH503 |
| B | HOH508 |
| B | HOH518 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | HOH590 |
| B | ASP296 |
| B | LEU297 |
| B | MET298 |
| B | HOH526 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | LYS32 |
| B | PRO33 |
| B | SER94 |
| B | ASN97 |
| B | LYS98 |
| B | LEU99 |
| B | PRO100 |
| site_id | AE9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | THR43 |
| B | SER67 |
| B | PRO69 |
| B | PHE71 |
| B | HOH510 |
| site_id | AF1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 410 |
| Chain | Residue |
| B | THR165 |
| B | ASN169 |
| B | PHE304 |
| B | ALA305 |
| B | VAL306 |
| B | LYS308 |
| B | HOH573 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 411 |
| Chain | Residue |
| B | THR40 |
| B | SER105 |
| B | ASP134 |
| B | GLN157 |
| site_id | AF3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 412 |
| Chain | Residue |
| B | ILE222 |
| B | ASP223 |
| B | PRO260 |
| site_id | AF4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 413 |
| Chain | Residue |
| B | PRO54 |
| B | ASP265 |
| B | GLN270 |
| site_id | AF5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 414 |
| Chain | Residue |
| A | GLN175 |
| A | ILE176 |
| B | ALA92 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 415 |
| Chain | Residue |
| B | TYR203 |
| B | ASN206 |
| B | HOH607 |
| site_id | AF7 |
| Number of Residues | 5 |
| Details | binding site for residue PGE B 417 |
| Chain | Residue |
| B | ASN292 |
| B | ARG309 |
| B | CYS311 |
| B | GLY313 |
| B | SO4403 |
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 |
