1KRE
STRUCTURE OF P. CITRINUM ALPHA 1,2-MANNOSIDASE REVEALS THE BASIS FOR DIFFERENCES IN SPECIFICITY OF THE ER AND GOLGI CLASS I ENZYMES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004571 | molecular_function | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016020 | cellular_component | membrane |
| B | 0004571 | molecular_function | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11714724 |
| Chain | Residue | Details |
| A | ASP375 | |
| B | ASP375 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45700 |
| Chain | Residue | Details |
| A | THR501 | |
| B | THR501 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11714724, ECO:0007744|PDB:1KKT, ECO:0007744|PDB:1KRE, ECO:0007744|PDB:1KRF, ECO:0007744|PDB:2RI8, ECO:0007744|PDB:2RI9 |
| Chain | Residue | Details |
| A | ASN182 | |
| A | ASN366 | |
| A | ASN438 | |
| B | ASN182 | |
| B | ASN366 | |
| B | ASN438 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dl2 |
| Chain | Residue | Details |
| A | ARG126 | |
| A | GLU122 | |
| A | GLU409 | |
| A | ASP267 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dl2 |
| Chain | Residue | Details |
| B | ARG126 | |
| B | GLU122 | |
| B | GLU409 | |
| B | ASP267 |
