1DL2
CRYSTAL STRUCTURE OF CLASS I ALPHA-1,2-MANNOSIDASE FROM SACCHAROMYCES CEREVISIAE AT 1.54 ANGSTROM RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004559 | molecular_function | alpha-mannosidase activity |
| A | 0004571 | molecular_function | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006486 | biological_process | obsolete protein glycosylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0035977 | biological_process | protein deglycosylation involved in glycoprotein catabolic process |
| A | 0036503 | biological_process | ERAD pathway |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P31723","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10675327","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2000","submissionDatabase":"PDB data bank","title":"Structure and function of Class I a1,2-mannosidases involved in glycoprotein biosynthesis.","authors":["Herscovics A.","Lipari F.","Sleno B.","Romera P.A.","Vallee F.","Yip P.","Howell P.A."]}},{"source":"PDB","id":"1G6I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 20141183, 20219151, 20576295 |
| Chain | Residue | Details |
| A | ARG136 | |
| A | GLU435 | |
| A | ASP275 | |
| A | GLU132 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 19 |
| Chain | Residue | Details |
| A | GLU132 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG136 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ASP275 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU435 | activator |
