1DEO
RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE
Functional Information from GO Data
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:10801485 |
| Chain | Residue | Details |
| A | SER9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:10801485 |
| Chain | Residue | Details |
| A | ASP192 | |
| A | HIS195 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 |
| Chain | Residue | Details |
| A | ASN104 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:10801485, ECO:0000269|PubMed:11752785, ECO:0000269|PubMed:18645234 |
| Chain | Residue | Details |
| A | ASN182 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 705 |
| Chain | Residue | Details |
| A | SER9 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY42 | electrostatic stabiliser |
| A | ASN74 | electrostatic stabiliser |
| A | ASP192 | electrostatic stabiliser, increase basicity |
| A | HIS195 | proton acceptor, proton donor |
