1OUW
Crystal structure of Calystegia sepium agglutinin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005536 | molecular_function | D-glucose binding |
| A | 0005537 | molecular_function | D-mannose binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045840 | biological_process | positive regulation of mitotic nuclear division |
| A | 0050839 | molecular_function | cell adhesion molecule binding |
| B | 0005536 | molecular_function | D-glucose binding |
| B | 0005537 | molecular_function | D-mannose binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045840 | biological_process | positive regulation of mitotic nuclear division |
| B | 0050839 | molecular_function | cell adhesion molecule binding |
| C | 0005536 | molecular_function | D-glucose binding |
| C | 0005537 | molecular_function | D-mannose binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0045840 | biological_process | positive regulation of mitotic nuclear division |
| C | 0050839 | molecular_function | cell adhesion molecule binding |
| D | 0005536 | molecular_function | D-glucose binding |
| D | 0005537 | molecular_function | D-mannose binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0007157 | biological_process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0045840 | biological_process | positive regulation of mitotic nuclear division |
| D | 0050839 | molecular_function | cell adhesion molecule binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLT D 501 |
| Chain | Residue |
| A | LYS109 |
| D | HOH885 |
| D | HOH1121 |
| D | HOH1166 |
| D | GLY91 |
| D | ILE92 |
| D | ARG100 |
| D | VAL118 |
| D | GLY119 |
| D | HOH653 |
| D | HOH846 |
| D | HOH847 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLT C 502 |
| Chain | Residue |
| B | LYS109 |
| C | GLY91 |
| C | ILE92 |
| C | ARG100 |
| C | VAL118 |
| C | GLY119 |
| C | HOH683 |
| C | HOH830 |
| C | HOH942 |
| C | HOH1062 |
| C | HOH1122 |
| C | HOH1138 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | GLY140 |
| A | TYR141 |
| A | TYR142 |
| A | ASP144 |
| A | IMD523 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 511 |
| Chain | Residue |
| B | PRO66 |
| B | TYR141 |
| B | HOH739 |
| C | ASN96 |
| C | GLY140 |
| C | TYR141 |
| C | TYR142 |
| C | ASP144 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 512 |
| Chain | Residue |
| A | PRO66 |
| A | TYR141 |
| A | EDO515 |
| D | ASN96 |
| D | GLY140 |
| D | TYR141 |
| D | TYR142 |
| D | ASP144 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 513 |
| Chain | Residue |
| B | GLY140 |
| B | TYR141 |
| B | TYR142 |
| B | ASP144 |
| B | IMD520 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 514 |
| Chain | Residue |
| A | GLY54 |
| A | SER55 |
| A | LYS56 |
| A | HOH908 |
| B | MET5 |
| B | HOH931 |
| B | HOH1191 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 515 |
| Chain | Residue |
| A | GLY64 |
| A | GLY65 |
| A | PRO66 |
| D | ASN96 |
| D | TYR141 |
| D | EDO512 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 516 |
| Chain | Residue |
| A | ARG138 |
| B | MET5 |
| B | ASP6 |
| B | HOH626 |
| B | HOH951 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO D 517 |
| Chain | Residue |
| C | ILE8 |
| C | SER55 |
| C | LYS56 |
| D | MET5 |
| D | HOH1036 |
| D | HOH1085 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 518 |
| Chain | Residue |
| C | TRP12 |
| C | GLY13 |
| C | THR72 |
| C | MET74 |
| C | HOH832 |
| C | HOH1176 |
| D | AYA2 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD B 520 |
| Chain | Residue |
| B | TYR141 |
| B | TYR142 |
| B | EDO513 |
| C | ASN15 |
| C | GLY17 |
| C | HOH1098 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 521 |
| Chain | Residue |
| A | VAL25 |
| A | ASN26 |
| A | LYS27 |
| A | GLU131 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD B 522 |
| Chain | Residue |
| B | VAL25 |
| B | ASN26 |
| B | LYS27 |
| B | GLU131 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD A 523 |
| Chain | Residue |
| D | GLY17 |
| A | ASN96 |
| A | TYR141 |
| A | EDO510 |
| D | ASN15 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:14561768, ECO:0007744|PDB:1OUW |
| Chain | Residue | Details |
| A | AYA2 | |
| B | AYA2 | |
| C | AYA2 | |
| D | AYA2 |
