3CEL
ACTIVE-SITE MUTANT E212Q DETERMINED AT PH 6.0 WITH CELLOBIOSE BOUND IN THE ACTIVE SITE
Functional Information from GO Data
Functional Information from PDB Data
| site_id | CAD |
| Number of Residues | 3 |
| Details | CALCIUM-BINDING SITE ON CRYSTALLOGRAPHIC DYAD. NOTE THAT THE CADMIUM ION IS BOUND BY GLU 295 AND GLU 325 FROM TWO CRYSTALLOGRAPHICALLY RELATED MOLECULES. |
| Chain | Residue |
| A | CD1000 |
| A | GLU295 |
| A | GLU325 |
| site_id | CTA |
| Number of Residues | 4 |
| Details | CATALYTIC SITE INCLUDING MUTATION E212Q. |
| Chain | Residue |
| A | GLN212 |
| A | ASP214 |
| A | GLU217 |
| A | HIS228 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8036495","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"24341799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9466911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9746354","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1cel |
| Chain | Residue | Details |
| A | GLN212 | |
| A | HIS228 | |
| A | ASP214 | |
| A | GLU217 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 444 |
| Chain | Residue | Details |
| A | TRP216 | covalent catalysis |
| A | ALA218 | modifies pKa |
| A | ILE221 | proton shuttle (general acid/base) |
| A | THR232 | modifies pKa |
