Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005537 | molecular_function | D-mannose binding |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0046872 | molecular_function | metal ion binding |
C | 0005537 | molecular_function | D-mannose binding |
C | 0030246 | molecular_function | carbohydrate binding |
C | 0046872 | molecular_function | metal ion binding |
E | 0005537 | molecular_function | D-mannose binding |
E | 0030246 | molecular_function | carbohydrate binding |
E | 0046872 | molecular_function | metal ion binding |
G | 0005537 | molecular_function | D-mannose binding |
G | 0030246 | molecular_function | carbohydrate binding |
G | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 238 |
Chain | Residue |
A | GLU8 |
A | ASP10 |
A | ASP19 |
A | HIS24 |
A | HOH289 |
A | HOH494 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 239 |
Chain | Residue |
A | ASP19 |
A | HOH259 |
A | HOH503 |
A | ASP10 |
A | TYR12 |
A | ASN14 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 238 |
Chain | Residue |
C | GLU8 |
C | ASP10 |
C | ASP19 |
C | HIS24 |
C | HOH537 |
C | HOH556 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 239 |
Chain | Residue |
C | ASP10 |
C | TYR12 |
C | ASN14 |
C | ASP19 |
C | HOH256 |
C | HOH536 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 238 |
Chain | Residue |
E | GLU8 |
E | ASP10 |
E | ASP19 |
E | HIS24 |
E | HOH545 |
E | HOH557 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 239 |
Chain | Residue |
E | ASP10 |
E | TYR12 |
E | ASN14 |
E | ASP19 |
E | HOH269 |
E | HOH304 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ABA E 240 |
Chain | Residue |
E | TRP88 |
E | ASN124 |
E | ALA125 |
E | HIS180 |
E | HOH540 |
E | HOH553 |
E | HOH558 |
G | PHE128 |
G | SER129 |
G | PHE130 |
G | ASP139 |
G | HOH319 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN G 238 |
Chain | Residue |
G | GLU8 |
G | ASP10 |
G | ASP19 |
G | HIS24 |
G | HOH546 |
G | HOH547 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA G 239 |
Chain | Residue |
G | ASP10 |
G | TYR12 |
G | ASN14 |
G | ASP19 |
G | HOH323 |
G | HOH538 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ABA G 240 |
Chain | Residue |
E | PHE130 |
E | ASP139 |
G | SER113 |
G | LYS114 |
G | ALA125 |
G | LEU126 |
G | VAL179 |
G | HIS180 |
G | HOH254 |
G | HOH302 |
Functional Information from PROSITE/UniProt
site_id | PS00307 |
Number of Residues | 7 |
Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVELDS |
Chain | Residue | Details |
A | VAL5-SER11 | |
site_id | PS00308 |
Number of Residues | 10 |
Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGLS |
Chain | Residue | Details |
A | LEU85-SER94 | |