Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005537 | molecular_function | D-mannose binding |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0046872 | molecular_function | metal ion binding |
A | 0090729 | molecular_function | toxin activity |
B | 0005537 | molecular_function | D-mannose binding |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0046872 | molecular_function | metal ion binding |
B | 0090729 | molecular_function | toxin activity |
C | 0005537 | molecular_function | D-mannose binding |
C | 0030246 | molecular_function | carbohydrate binding |
C | 0035821 | biological_process | modulation of process of another organism |
C | 0046872 | molecular_function | metal ion binding |
C | 0090729 | molecular_function | toxin activity |
D | 0005537 | molecular_function | D-mannose binding |
D | 0030246 | molecular_function | carbohydrate binding |
D | 0035821 | biological_process | modulation of process of another organism |
D | 0046872 | molecular_function | metal ion binding |
D | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | GLU8 |
A | ASP10 |
A | ASP19 |
A | HIS24 |
A | HOH411 |
A | HOH414 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | ASP19 |
A | ASP10 |
A | TYR12 |
A | ASN14 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 403 |
Chain | Residue |
B | GLU8 |
B | ASP10 |
B | ASP19 |
B | HIS24 |
B | HOH415 |
B | HOH417 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 404 |
Chain | Residue |
B | ASP10 |
B | TYR12 |
B | ASN14 |
B | ASP19 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 405 |
Chain | Residue |
C | GLU8 |
C | ASP10 |
C | ASP19 |
C | HIS24 |
C | HOH416 |
C | HOH419 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 406 |
Chain | Residue |
C | ASP10 |
C | TYR12 |
C | ASN14 |
C | ASP19 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 407 |
Chain | Residue |
D | GLU8 |
D | ASP10 |
D | ASP19 |
D | HIS24 |
D | HOH411 |
D | HOH419 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA D 408 |
Chain | Residue |
D | ASP10 |
D | TYR12 |
D | ASN14 |
D | ASP19 |
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 | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU8 | |
B | TYR12 | |
B | ASN14 | |
B | ASP19 | |
B | HIS24 | |
B | LEU99 | |
C | GLU8 | |
C | ASP10 | |
C | TYR12 | |
C | ASN14 | |
C | ASP19 | |
A | ASP10 | |
C | HIS24 | |
C | LEU99 | |
D | GLU8 | |
D | ASP10 | |
D | TYR12 | |
D | ASN14 | |
D | ASP19 | |
D | HIS24 | |
D | LEU99 | |
A | TYR12 | |
A | ASN14 | |
A | ASP19 | |
A | HIS24 | |
A | LEU99 | |
B | GLU8 | |
B | ASP10 | |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER34 | |
A | ASP208 | |
B | SER34 | |
B | ASP208 | |
C | SER34 | |
C | ASP208 | |
D | SER34 | |
D | ASP208 | |
Chain | Residue | Details |
A | ARG228 | |
B | ARG228 | |
C | ARG228 | |
D | ARG228 | |