1VCL
Crystal Structure of Hemolytic Lectin CEL-III
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001906 | biological_process | cell killing |
| A | 0004653 | molecular_function | polypeptide N-acetylgalactosaminyltransferase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005534 | molecular_function | galactose binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006493 | biological_process | protein O-linked glycosylation |
| A | 0019731 | biological_process | antibacterial humoral response |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0030395 | molecular_function | lactose binding |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0034120 | biological_process | positive regulation of erythrocyte aggregation |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042806 | molecular_function | fucose binding |
| A | 0044179 | biological_process | hemolysis in another organism |
| A | 0046871 | molecular_function | N-acetylgalactosamine binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050829 | biological_process | defense response to Gram-negative bacterium |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| A | 0051260 | biological_process | protein homooligomerization |
| A | 0051673 | biological_process | disruption of plasma membrane integrity in another organism |
| A | 1903777 | molecular_function | melibiose binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001906 | biological_process | cell killing |
| B | 0004653 | molecular_function | polypeptide N-acetylgalactosaminyltransferase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005534 | molecular_function | galactose binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006493 | biological_process | protein O-linked glycosylation |
| B | 0019731 | biological_process | antibacterial humoral response |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0030395 | molecular_function | lactose binding |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0034120 | biological_process | positive regulation of erythrocyte aggregation |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0042806 | molecular_function | fucose binding |
| B | 0044179 | biological_process | hemolysis in another organism |
| B | 0046871 | molecular_function | N-acetylgalactosamine binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050829 | biological_process | defense response to Gram-negative bacterium |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0051260 | biological_process | protein homooligomerization |
| B | 0051673 | biological_process | disruption of plasma membrane integrity in another organism |
| B | 1903777 | molecular_function | melibiose binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 1001 |
| Chain | Residue |
| A | ASP23 |
| A | ILE24 |
| A | GLY26 |
| A | ASP43 |
| A | HOH1337 |
| A | HOH1550 |
| A | HOH1681 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 1002 |
| Chain | Residue |
| A | GLY124 |
| A | ASP141 |
| A | HOH1559 |
| A | HOH1652 |
| A | HOH1664 |
| A | ASP121 |
| A | ILE122 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1003 |
| Chain | Residue |
| A | ASP168 |
| A | VAL169 |
| A | GLY171 |
| A | ASP188 |
| A | HOH1587 |
| A | HOH1710 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1004 |
| Chain | Residue |
| A | ASP209 |
| A | VAL210 |
| A | GLY212 |
| A | ASP229 |
| A | HOH1704 |
| A | HOH1709 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 1005 |
| Chain | Residue |
| A | ASP256 |
| A | VAL257 |
| A | GLY259 |
| A | ASP276 |
| A | HOH1363 |
| A | HOH1379 |
| A | HOH1437 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1101 |
| Chain | Residue |
| A | ASN32 |
| A | ILE33 |
| A | ASN72 |
| A | VAL73 |
| A | ILE131 |
| A | HOH1390 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1102 |
| Chain | Residue |
| A | ASN177 |
| A | VAL178 |
| A | ASN218 |
| A | VAL219 |
| A | ASP265 |
| A | VAL266 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1001 |
| Chain | Residue |
| B | ASP23 |
| B | ILE24 |
| B | GLY26 |
| B | ASP43 |
| B | HOH2606 |
| B | HOH2608 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1002 |
| Chain | Residue |
| B | ASP121 |
| B | ILE122 |
| B | GLY124 |
| B | ASP141 |
| B | HOH2584 |
| B | HOH2588 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1003 |
| Chain | Residue |
| B | ASP168 |
| B | VAL169 |
| B | GLY171 |
| B | ASP188 |
| B | HOH2605 |
| B | HOH2617 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1004 |
| Chain | Residue |
| B | ASP209 |
| B | VAL210 |
| B | GLY212 |
| B | ASP229 |
| B | HOH2604 |
| B | HOH2616 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 1005 |
| Chain | Residue |
| B | ASP256 |
| B | VAL257 |
| B | GLY259 |
| B | ASP276 |
| B | HOH2225 |
| B | HOH2264 |
| B | HOH2340 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1101 |
| Chain | Residue |
| B | ASN32 |
| B | ILE33 |
| B | ASN72 |
| B | VAL73 |
| B | ILE131 |
| B | HOH2607 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1102 |
| Chain | Residue |
| B | ASN177 |
| B | VAL178 |
| B | ASN218 |
| B | VAL219 |
| B | ASP265 |
| B | VAL266 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1201 |
| Chain | Residue |
| A | GLY212 |
| A | SER213 |
| A | ASP214 |
| A | LYS338 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 2201 |
| Chain | Residue |
| B | GLY212 |
| B | SER213 |
| B | ASP214 |
| B | LYS338 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BTB A 1301 |
| Chain | Residue |
| A | ALA352 |
| A | ASN355 |
| A | SER356 |
| A | GLN402 |
| A | HOH1381 |
| A | HOH1516 |
| A | CYS4 |
| A | PRO7 |
| A | GLU57 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17977832, ECO:0007744|PDB:2Z48 |
| Chain | Residue | Details |
| A | ASP9 | |
| A | VAL107 | |
| B | ASP9 | |
| B | VAL107 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T |
| Chain | Residue | Details |
| A | ASP23 | |
| A | ILE122 | |
| A | GLY124 | |
| A | ILE131 | |
| A | ASP141 | |
| A | ASP168 | |
| A | VAL169 | |
| A | GLY171 | |
| A | ASN177 | |
| A | VAL178 | |
| A | ASP188 | |
| A | ILE24 | |
| A | ASP209 | |
| A | VAL210 | |
| A | GLY212 | |
| A | ASN218 | |
| A | VAL219 | |
| A | ASP229 | |
| A | ASP256 | |
| A | VAL257 | |
| A | GLY259 | |
| A | ASP265 | |
| A | GLY26 | |
| A | VAL266 | |
| B | ASP23 | |
| B | ILE24 | |
| B | GLY26 | |
| B | ASN32 | |
| B | ILE33 | |
| B | ASP43 | |
| B | ASN72 | |
| B | VAL73 | |
| B | ASP121 | |
| A | ASN32 | |
| B | ILE122 | |
| B | GLY124 | |
| B | ILE131 | |
| B | ASP141 | |
| B | ASP168 | |
| B | VAL169 | |
| B | GLY171 | |
| B | ASN177 | |
| B | VAL178 | |
| B | ASP188 | |
| A | ILE33 | |
| B | ASP209 | |
| B | VAL210 | |
| B | GLY212 | |
| B | ASN218 | |
| B | VAL219 | |
| B | ASP229 | |
| B | ASP256 | |
| B | VAL257 | |
| B | GLY259 | |
| B | ASP265 | |
| A | ASP43 | |
| B | VAL266 | |
| A | ASN72 | |
| A | VAL73 | |
| A | ASP121 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T |
| Chain | Residue | Details |
| A | ASP39 | |
| A | TRP269 | |
| A | ASP276 | |
| B | ASP39 | |
| B | TRP269 | |
| B | ASP276 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T |
| Chain | Residue | Details |
| A | TYR134 | |
| A | TYR181 | |
| A | TYR222 | |
| B | TYR134 | |
| B | TYR181 | |
| B | TYR222 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:10561549, ECO:0000269|PubMed:15194688 |
| Chain | Residue | Details |
| A | PCA1 | |
| B | PCA1 |
