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: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP208 | |
B | ASP208 | |
C | ASP208 | |
D | ASP208 | |
Chain | Residue | Details |
A | ARG228 | |
A | LEU99 | |
B | ARG228 | |
B | LEU99 | |
C | ARG228 | |
C | LEU99 | |
D | ARG228 | |
D | LEU99 | |
Chain | Residue | Details |
A | GLU8 | |
C | ASP10 | |
C | ASP19 | |
C | HIS24 | |
D | GLU8 | |
D | ASP10 | |
D | ASP19 | |
D | HIS24 | |
A | ASP10 | |
A | ASP19 | |
A | HIS24 | |
B | GLU8 | |
B | ASP10 | |
B | ASP19 | |
B | HIS24 | |
C | GLU8 | |
Chain | Residue | Details |
A | TYR12 | |
A | ASN14 | |
B | TYR12 | |
B | ASN14 | |
C | TYR12 | |
C | ASN14 | |
D | TYR12 | |
D | ASN14 | |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | SITE: Cleavage |
Chain | Residue | Details |
A | ASN237 | |
A | ASN118 | |
B | ASN237 | |
B | ASN118 | |
C | ASN237 | |
C | ASN118 | |
D | ASN237 | |
D | ASN118 | |