Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | GLU118 |
A | ASP120 |
A | GLU129 |
A | HIS134 |
A | HOH429 |
A | HOH458 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 302 |
Chain | Residue |
A | GLU129 |
A | HOH455 |
A | HOH462 |
A | ASP120 |
A | TRP122 |
A | ASN124 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | PHE5 |
A | ASN6 |
A | ASP15 |
A | TYR50 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | SER224 |
A | THR226 |
A | HOH537 |
B | ASN185 |
B | EDO304 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | TYR97 |
A | PRO103 |
A | ALA106 |
A | TRP127 |
A | HOH507 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | ILE39 |
A | PRO40 |
A | THR72 |
A | TYR213 |
A | HOH423 |
A | HOH562 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ASP78 |
A | GLY96 |
A | TRP122 |
A | ASN124 |
A | GLY211 |
A | HOH532 |
A | HOH540 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA B 301 |
Chain | Residue |
B | GLU118 |
B | ASP120 |
B | GLU129 |
B | HIS134 |
B | HOH451 |
B | HOH458 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue CA B 302 |
Chain | Residue |
B | ASP120 |
B | TRP122 |
B | ASN124 |
B | GLU129 |
B | HOH441 |
B | HOH445 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
A | ASN185 |
B | TYR62 |
B | SER224 |
B | THR226 |
B | HOH405 |
B | HOH518 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | SER60 |
A | EDO304 |
B | ARG146 |
B | THR148 |
B | TYR186 |
B | VAL187 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | ASP78 |
B | GLY96 |
B | TRP122 |
B | ASN124 |
B | GLY211 |
B | HOH434 |
B | HOH521 |
Functional Information from PROSITE/UniProt
site_id | PS00307 |
Number of Residues | 7 |
Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT |
Chain | Residue | Details |
A | VAL115-THR121 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | TRP122 | |
B | ASN124 | |
B | GLU129 | |
B | HIS134 | |
A | GLU118 | |
A | ASP120 | |
A | TRP122 | |
A | ASN124 | |
A | GLU129 | |
A | HIS134 | |
B | GLU118 | |
B | ASP120 | |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.1 |
Chain | Residue | Details |
A | ASN26 | |
A | ASN108 | |
B | ASN26 | |
B | ASN108 | |