Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005537 | molecular_function | D-mannose binding |
A | 0030246 | molecular_function | carbohydrate binding |
B | 0005537 | molecular_function | D-mannose binding |
B | 0030246 | molecular_function | carbohydrate binding |
C | 0005537 | molecular_function | D-mannose binding |
C | 0030246 | molecular_function | carbohydrate binding |
D | 0005537 | molecular_function | D-mannose binding |
D | 0030246 | molecular_function | carbohydrate binding |
E | 0005537 | molecular_function | D-mannose binding |
E | 0030246 | molecular_function | carbohydrate binding |
F | 0005537 | molecular_function | D-mannose binding |
F | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 301 |
Chain | Residue |
A | GLU123 |
A | ASP125 |
A | ASP133 |
A | HIS138 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 302 |
Chain | Residue |
A | ASP125 |
A | PHE127 |
A | ASN129 |
A | ASP133 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 301 |
Chain | Residue |
B | ASP125 |
B | ASP133 |
B | HIS138 |
B | SER148 |
B | GLU123 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA B 302 |
Chain | Residue |
B | ASP125 |
B | PHE127 |
B | ASN129 |
B | ASP133 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN C 301 |
Chain | Residue |
C | GLU123 |
C | ASP125 |
C | ASP133 |
C | HIS138 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 302 |
Chain | Residue |
C | ASP125 |
C | PHE127 |
C | ASN129 |
C | ASP133 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN D 301 |
Chain | Residue |
D | GLU123 |
D | ASP125 |
D | ASP133 |
D | HIS138 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA D 302 |
Chain | Residue |
D | ASP125 |
D | PHE127 |
D | ASN129 |
D | ASP133 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN E 301 |
Chain | Residue |
E | GLU123 |
E | ASP125 |
E | ASP133 |
E | HIS138 |
E | SER148 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA E 302 |
Chain | Residue |
E | ASP125 |
E | PHE127 |
E | ASN129 |
E | ASP133 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN F 301 |
Chain | Residue |
F | GLU123 |
F | ASP125 |
F | ASP133 |
F | HIS138 |
F | SER148 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA F 302 |
Chain | Residue |
F | ASP125 |
F | PHE127 |
F | ASN129 |
F | ASP133 |
Functional Information from PROSITE/UniProt
site_id | PS00307 |
Number of Residues | 7 |
Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT |
Chain | Residue | Details |
A | VAL120-THR126 | |
site_id | PS00308 |
Number of Residues | 10 |
Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEYVSIGFS |
Chain | Residue | Details |
A | LEU200-SER209 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN12 | |
E | ASN79 | |
F | ASN12 | |
F | ASN79 | |
A | ASN79 | |
B | ASN12 | |
B | ASN79 | |
C | ASN12 | |
C | ASN79 | |
D | ASN12 | |
D | ASN79 | |
E | ASN12 | |