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 |