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 | 17 |
Details | binding site for residue QTY A 301 |
Chain | Residue |
A | ASP80 |
A | HOH410 |
A | HOH424 |
A | HOH454 |
A | HOH466 |
A | HOH477 |
A | HOH480 |
B | LEU212 |
B | HOH488 |
A | ASP83 |
A | GLY103 |
A | GLY104 |
A | TYR125 |
A | ASN127 |
A | SER211 |
A | GLY213 |
A | GLY214 |
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 | HOH402 |
A | HOH426 |
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 | HOH460 |
A | HOH530 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue QTY B 301 |
Chain | Residue |
B | ASP80 |
B | ASP83 |
B | GLY103 |
B | GLY104 |
B | TYR125 |
B | ASN127 |
B | SER211 |
B | GLY214 |
B | HOH401 |
B | HOH408 |
B | HOH429 |
B | HOH547 |
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 | HOH403 |
B | HOH405 |
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 | HOH485 |
B | HOH516 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue QTY C 301 |
Chain | Residue |
C | ASP80 |
C | ASP83 |
C | GLY103 |
C | GLY104 |
C | TYR125 |
C | ASN127 |
C | SER211 |
C | GLY214 |
C | HOH450 |
C | HOH453 |
C | HOH478 |
C | HOH506 |
C | HOH537 |
site_id | AC8 |
Number of Residues | 13 |
Details | binding site for residue QTY D 301 |
Chain | Residue |
D | ASP80 |
D | ASP83 |
D | GLY103 |
D | GLY104 |
D | TYR125 |
D | ASN127 |
D | SER211 |
D | GLY214 |
D | HOH416 |
D | HOH422 |
D | HOH461 |
D | HOH484 |
D | HOH508 |
site_id | AC9 |
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 | HOH420 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue CA D 303 |
Chain | Residue |
D | ASP123 |
D | TYR125 |
D | ASN127 |
D | ASP132 |
D | HOH414 |
D | HOH464 |
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 | |