1FHL
CRYSTAL STRUCTURE OF BETA-1,4-GALACTANASE FROM ASPERGILLUS ACULEATUS AT 293K
Functional Information from GO Data
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 12484750 |
| Chain | Residue | Details |
| A | GLU136 | |
| A | GLU246 | |
| A | ARG45 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 658 |
| Chain | Residue | Details |
| A | ARG45 | electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity, modifies pKa |
| A | GLU136 | activator, increase nucleophilicity, proton acceptor, proton donor |
| A | GLU246 | covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile |
