3IPV
Crystal structure of Spatholobus parviflorus seed lectin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005534 | molecular_function | galactose binding |
| A | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0030395 | molecular_function | lactose binding |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050832 | biological_process | defense response to fungus |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005534 | molecular_function | galactose binding |
| B | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0030395 | molecular_function | lactose binding |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050832 | biological_process | defense response to fungus |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005534 | molecular_function | galactose binding |
| C | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0030395 | molecular_function | lactose binding |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050832 | biological_process | defense response to fungus |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005534 | molecular_function | galactose binding |
| D | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0030395 | molecular_function | lactose binding |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 252 |
| Chain | Residue |
| A | ASP128 |
| A | TYR130 |
| A | ASN132 |
| A | ASP137 |
| A | HOH314 |
| A | HOH321 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 253 |
| Chain | Residue |
| A | HIS142 |
| A | HOH332 |
| A | HOH333 |
| A | GLU126 |
| A | ASP128 |
| A | ASP137 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 240 |
| Chain | Residue |
| B | ASP128 |
| B | TYR130 |
| B | ASN132 |
| B | ASP137 |
| B | HOH295 |
| B | HOH527 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 241 |
| Chain | Residue |
| B | GLU126 |
| B | ASP128 |
| B | ASP137 |
| B | HIS142 |
| B | HOH291 |
| B | HOH609 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 252 |
| Chain | Residue |
| C | ASP128 |
| C | TYR130 |
| C | ASN132 |
| C | ASP137 |
| C | HOH310 |
| C | HOH316 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 253 |
| Chain | Residue |
| C | GLU126 |
| C | ASP128 |
| C | ASP137 |
| C | HIS142 |
| C | HOH266 |
| C | HOH677 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 240 |
| Chain | Residue |
| D | ASP128 |
| D | TYR130 |
| D | ASN132 |
| D | ASP137 |
| D | HOH307 |
| D | HOH321 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 241 |
| Chain | Residue |
| D | GLU126 |
| D | ASP128 |
| D | ASP137 |
| D | HIS142 |
| D | HOH287 |
| D | HOH551 |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VFTDPPY |
| Chain | Residue | Details |
| B | VAL134-TYR140 | |
| A | VAL134-TYR140 |
| site_id | PS00307 |
| Number of Residues | 7 |
| Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT |
| Chain | Residue | Details |
| B | VAL123-THR129 | |
| A | VAL123-THR129 |
| site_id | PS00308 |
| Number of Residues | 10 |
| Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVRVGFS |
| Chain | Residue | Details |
| B | LEU204-SER213 | |
| A | LEU204-SER213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P02870 |
| Chain | Residue | Details |
| B | ASP88 | |
| D | ASP88 | |
| D | GLY106 | |
| D | GLU126 | |
| D | ASP128 | |
| D | ASN132 | |
| D | ASP137 | |
| D | HIS142 | |
| D | GLY217 | |
| D | ALA218 | |
| B | GLY106 | |
| B | GLU126 | |
| B | ASP128 | |
| B | ASN132 | |
| B | ASP137 | |
| B | HIS142 | |
| B | GLY217 | |
| B | ALA218 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21889532, ECO:0007744|PDB:3IPV, ECO:0007744|PDB:4M3C |
| Chain | Residue | Details |
| A | GLU126 | |
| C | ASN132 | |
| C | ASP137 | |
| C | HIS142 | |
| A | ASP128 | |
| A | TYR130 | |
| A | ASN132 | |
| A | ASP137 | |
| A | HIS142 | |
| C | GLU126 | |
| C | ASP128 | |
| C | TYR130 |
