Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005537 | molecular_function | D-mannose binding |
| A | 0006952 | biological_process | defense response |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050688 | biological_process | regulation of defense response to virus |
| B | 0005537 | molecular_function | D-mannose binding |
| B | 0006952 | biological_process | defense response |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050688 | biological_process | regulation of defense response to virus |
| C | 0005537 | molecular_function | D-mannose binding |
| C | 0006952 | biological_process | defense response |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050688 | biological_process | regulation of defense response to virus |
| D | 0005537 | molecular_function | D-mannose binding |
| D | 0006952 | biological_process | defense response |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050688 | biological_process | regulation of defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue R3M A 301 |
| Chain | Residue |
| A | TYR12 |
| A | HOH426 |
| B | R3M301 |
| A | ASN14 |
| A | ASP16 |
| A | GLY98 |
| A | LEU99 |
| A | TYR100 |
| A | ALA207 |
| A | ASP208 |
| A | ARG228 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 302 |
| Chain | Residue |
| A | GLU8 |
| A | ASP10 |
| A | ASP19 |
| A | HIS24 |
| A | HOH413 |
| A | HOH414 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | ASP10 |
| A | TYR12 |
| A | ASN14 |
| A | ASP19 |
| A | HOH415 |
| A | HOH416 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue R3M B 301 |
| Chain | Residue |
| A | TYR100 |
| A | HIS205 |
| A | R3M301 |
| A | HOH405 |
| B | TYR12 |
| B | ASN14 |
| B | GLY98 |
| B | LEU99 |
| B | TYR100 |
| B | ALA207 |
| B | ASP208 |
| B | GLY227 |
| B | ARG228 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 302 |
| Chain | Residue |
| B | GLU8 |
| B | ASP10 |
| B | ASP19 |
| B | HIS24 |
| B | HOH406 |
| B | HOH407 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 303 |
| Chain | Residue |
| B | ASP10 |
| B | TYR12 |
| B | ASN14 |
| B | ASP19 |
| B | HOH408 |
| B | HOH409 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue R3M C 301 |
| Chain | Residue |
| C | TYR12 |
| C | ASN14 |
| C | ASP16 |
| C | GLY98 |
| C | LEU99 |
| C | TYR100 |
| C | ALA207 |
| C | ASP208 |
| C | GLY227 |
| C | ARG228 |
| C | HOH424 |
| D | LEU99 |
| D | R3M301 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 302 |
| Chain | Residue |
| C | GLU8 |
| C | ASP10 |
| C | ASP19 |
| C | HIS24 |
| C | HOH405 |
| C | HOH406 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 303 |
| Chain | Residue |
| C | ASP10 |
| C | TYR12 |
| C | ASN14 |
| C | ASP19 |
| C | HOH407 |
| C | HOH408 |
| site_id | AD1 |
| Number of Residues | 13 |
| Details | binding site for residue R3M D 301 |
| Chain | Residue |
| C | TYR100 |
| C | HIS205 |
| C | R3M301 |
| D | TYR12 |
| D | ASN14 |
| D | GLY98 |
| D | LEU99 |
| D | TYR100 |
| D | ALA207 |
| D | ASP208 |
| D | GLY227 |
| D | ARG228 |
| D | HOH401 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 302 |
| Chain | Residue |
| D | GLU8 |
| D | ASP10 |
| D | ASP19 |
| D | HIS24 |
| D | HOH403 |
| D | HOH408 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 303 |
| Chain | Residue |
| D | ASP10 |
| D | TYR12 |
| D | ASN14 |
| D | ASP19 |
| D | HOH402 |
| D | HOH410 |
Functional Information from PROSITE/UniProt
| site_id | PS00307 |
| Number of Residues | 7 |
| Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDT |
| Chain | Residue | Details |
| A | VAL5-THR11 | |
| site_id | PS00308 |
| Number of Residues | 10 |
| Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS |
| Chain | Residue | Details |
| A | LEU85-SER94 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P81461","evidenceCode":"ECO:0000250"}]} |