1FAT
PHYTOHEMAGGLUTININ-L
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 | 0035821 | biological_process | modulation of process of another organism |
| A | 0090729 | molecular_function | toxin activity |
| B | 0005537 | molecular_function | D-mannose binding |
| B | 0006952 | biological_process | defense response |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0035821 | biological_process | modulation of process of another organism |
| B | 0090729 | molecular_function | toxin activity |
| C | 0005537 | molecular_function | D-mannose binding |
| C | 0006952 | biological_process | defense response |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0035821 | biological_process | modulation of process of another organism |
| C | 0090729 | molecular_function | toxin activity |
| D | 0005537 | molecular_function | D-mannose binding |
| D | 0006952 | biological_process | defense response |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
| site_id | CAA |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN CHAIN A |
| Chain | Residue |
| A | ASP124 |
| A | LEU126 |
| A | ASN128 |
| A | ASP132 |
| site_id | CAB |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN CHAIN B |
| Chain | Residue |
| B | LEU126 |
| B | ASN128 |
| B | ASP132 |
| B | ASP124 |
| site_id | CAC |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN CHAIN C |
| Chain | Residue |
| C | ASP124 |
| C | LEU126 |
| C | ASN128 |
| C | ASP132 |
| site_id | CAD |
| Number of Residues | 4 |
| Details | CALCIUM BINDING SITE IN CHAIN D |
| Chain | Residue |
| D | ASP124 |
| D | LEU126 |
| D | ASN128 |
| D | ASP132 |
| site_id | MNA |
| Number of Residues | 4 |
| Details | MANGANESE BINDING SITE IN CHAIN A |
| Chain | Residue |
| A | GLU122 |
| A | ASP124 |
| A | ASP132 |
| A | HIS137 |
| site_id | MNB |
| Number of Residues | 4 |
| Details | MANGANESE BINDING SITE IN CHAIN B |
| Chain | Residue |
| B | GLU122 |
| B | ASP124 |
| B | ASP132 |
| B | HIS137 |
| site_id | MNC |
| Number of Residues | 4 |
| Details | MANGANESE BINDING SITE IN CHAIN C |
| Chain | Residue |
| C | GLU122 |
| C | ASP124 |
| C | ASP132 |
| C | HIS137 |
| site_id | MND |
| Number of Residues | 4 |
| Details | MANGANESE BINDING SITE IN CHAIN D |
| Chain | Residue |
| D | GLU122 |
| D | ASP124 |
| D | ASP132 |
| D | HIS137 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","featureId":"CAR_000121","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1986","firstPage":"320","lastPage":"322","volume":"80","journal":"Plant Physiol.","title":"The high mannose oligosaccharide of phytohemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60.","authors":["Sturm A.","Chrispeels M.J."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000122","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1986","firstPage":"320","lastPage":"322","volume":"80","journal":"Plant Physiol.","title":"The high mannose oligosaccharide of phytohemagglutinin is attached to asparagine 12 and the modified oligosaccharide to asparagine 60.","authors":["Sturm A.","Chrispeels M.J."]}}]} |
| Chain | Residue | Details |
