Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0030246 | molecular_function | carbohydrate binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0030246 | molecular_function | carbohydrate binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue QWJ A 301 |
Chain | Residue |
A | ASP80 |
A | ASP83 |
A | GLY103 |
A | GLY104 |
A | TYR125 |
A | ASN127 |
A | SER211 |
A | GLY214 |
A | HOH401 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 302 |
Chain | Residue |
A | GLU121 |
A | ASP123 |
A | ASP132 |
A | HIS137 |
A | HOH405 |
A | HOH439 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 303 |
Chain | Residue |
A | ASP123 |
A | TYR125 |
A | ASN127 |
A | ASP132 |
A | HOH415 |
A | HOH477 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue QWJ B 301 |
Chain | Residue |
B | ASP80 |
B | ASP83 |
B | GLY103 |
B | GLY104 |
B | TYR125 |
B | ASN127 |
B | SER211 |
B | GLY214 |
B | HOH413 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MN B 302 |
Chain | Residue |
B | GLU121 |
B | ASP123 |
B | ASP132 |
B | HIS137 |
B | HOH415 |
B | HOH443 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA B 303 |
Chain | Residue |
B | ASP123 |
B | TYR125 |
B | ASN127 |
B | ASP132 |
B | HOH416 |
B | HOH434 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MN C 301 |
Chain | Residue |
C | GLU121 |
C | ASP123 |
C | ASP132 |
C | HIS137 |
C | HOH401 |
C | HOH415 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA C 302 |
Chain | Residue |
C | ASP123 |
C | TYR125 |
C | ASN127 |
C | ASP132 |
C | HOH411 |
C | HOH418 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue QWJ D 301 |
Chain | Residue |
D | ASP80 |
D | ASP83 |
D | GLY103 |
D | GLY104 |
D | TYR125 |
D | ASN127 |
D | SER211 |
D | GLY214 |
D | HOH429 |
D | HOH434 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MN D 302 |
Chain | Residue |
D | GLU121 |
D | ASP123 |
D | ASP132 |
D | HIS137 |
D | HOH401 |
D | HOH433 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue CA D 303 |
Chain | Residue |
D | ASP123 |
D | TYR125 |
D | ASN127 |
D | ASP132 |
D | HOH407 |
D | HOH445 |
Functional Information from PROSITE/UniProt
site_id | PS00307 |
Number of Residues | 7 |
Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VGVEFDT |
Chain | Residue | Details |
A | VAL118-THR124 | |
site_id | PS00308 |
Number of Residues | 10 |
Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPERVKFGFS |
Chain | Residue | Details |
A | LEU198-SER207 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU121 | |
B | ASN127 | |
B | ASP132 | |
B | HIS137 | |
C | GLU121 | |
C | ASP123 | |
C | TYR125 | |
C | ASN127 | |
C | ASP132 | |
C | HIS137 | |
D | GLU121 | |
A | ASP123 | |
D | ASP123 | |
D | TYR125 | |
D | ASN127 | |
D | ASP132 | |
D | HIS137 | |
A | TYR125 | |
A | ASN127 | |
A | ASP132 | |
A | HIS137 | |
B | GLU121 | |
B | ASP123 | |
B | TYR125 | |