4M3C
Structure of a binary complex between homologous tetrameric legume lectins from Butea monosperma and Spatholobus parviflorus seeds
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005534 | molecular_function | galactose binding |
| E | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| E | 0030145 | molecular_function | manganese ion binding |
| E | 0030246 | molecular_function | carbohydrate binding |
| E | 0030395 | molecular_function | lactose binding |
| E | 0031640 | biological_process | killing of cells of another organism |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050832 | biological_process | defense response to fungus |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005534 | molecular_function | galactose binding |
| F | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| F | 0030145 | molecular_function | manganese ion binding |
| F | 0030246 | molecular_function | carbohydrate binding |
| F | 0030395 | molecular_function | lactose binding |
| F | 0031640 | biological_process | killing of cells of another organism |
| F | 0032991 | cellular_component | protein-containing complex |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050832 | biological_process | defense response to fungus |
| G | 0005509 | molecular_function | calcium ion binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005534 | molecular_function | galactose binding |
| G | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| G | 0030145 | molecular_function | manganese ion binding |
| G | 0030246 | molecular_function | carbohydrate binding |
| G | 0030395 | molecular_function | lactose binding |
| G | 0031640 | biological_process | killing of cells of another organism |
| G | 0032991 | cellular_component | protein-containing complex |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050832 | biological_process | defense response to fungus |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005534 | molecular_function | galactose binding |
| H | 0015066 | molecular_function | alpha-amylase inhibitor activity |
| H | 0030145 | molecular_function | manganese ion binding |
| H | 0030246 | molecular_function | carbohydrate binding |
| H | 0030395 | molecular_function | lactose binding |
| H | 0031640 | biological_process | killing of cells of another organism |
| H | 0032991 | cellular_component | protein-containing complex |
| H | 0046872 | molecular_function | metal ion binding |
| H | 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 301 |
| Chain | Residue |
| A | ASP128 |
| A | TYR130 |
| A | ASN132 |
| A | ASP137 |
| A | HOH421 |
| A | HOH426 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 302 |
| Chain | Residue |
| A | HIS142 |
| A | HOH401 |
| A | HOH422 |
| A | GLU126 |
| A | ASP128 |
| A | ASP137 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ABU A 303 |
| Chain | Residue |
| A | ASN2 |
| A | THR3 |
| A | ASP4 |
| A | ILE57 |
| A | ASN58 |
| A | SER235 |
| D | THR7 |
| D | PHE8 |
| D | ASN17 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 301 |
| Chain | Residue |
| B | ASP128 |
| B | TYR130 |
| B | ASN132 |
| B | ASP137 |
| B | HOH430 |
| B | HOH434 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 302 |
| Chain | Residue |
| B | GLU126 |
| B | ASP128 |
| B | ASP137 |
| B | HIS142 |
| B | HOH420 |
| B | HOH435 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ABU B 303 |
| Chain | Residue |
| B | ASN2 |
| B | ASP4 |
| B | ILE57 |
| B | ASN58 |
| B | TRP207 |
| B | SER235 |
| B | LYS236 |
| B | HOH408 |
| C | ASN17 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 301 |
| Chain | Residue |
| C | ASP128 |
| C | TYR130 |
| C | ASN132 |
| C | ASP137 |
| C | HOH423 |
| C | HOH430 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 302 |
| Chain | Residue |
| C | GLU126 |
| C | ASP128 |
| C | ASP137 |
| C | HIS142 |
| C | HOH407 |
| C | HOH423 |
| C | HOH429 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ABU C 303 |
| Chain | Residue |
| B | ASN17 |
| B | HOH403 |
| B | HOH436 |
| C | ASN2 |
| C | ASP4 |
| C | ILE57 |
| C | ASN58 |
| C | TRP207 |
| C | SER235 |
| C | HOH426 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 304 |
| Chain | Residue |
| C | LEU52 |
| C | TYR53 |
| C | ALA54 |
| C | VAL97 |
| C | SER98 |
| C | SER209 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 301 |
| Chain | Residue |
| D | ASP128 |
| D | TYR130 |
| D | ASN132 |
| D | ASP137 |
| D | HOH413 |
| D | HOH420 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 302 |
| Chain | Residue |
| D | GLU126 |
| D | ASP128 |
| D | ASP137 |
| D | HIS142 |
| D | HOH425 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ABU D 303 |
| Chain | Residue |
| A | THR7 |
| A | PHE8 |
| A | LYS12 |
| A | GLN15 |
| A | ASN17 |
| D | ASN2 |
| D | THR3 |
| D | ASP4 |
| D | ASN58 |
| D | TRP207 |
| D | HOH409 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 304 |
| Chain | Residue |
| C | THR171 |
| C | VAL180 |
| D | HOH430 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 301 |
| Chain | Residue |
| E | ASP137 |
| E | HOH411 |
| E | HOH430 |
| E | ASP128 |
| E | TYR130 |
| E | ASN132 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 302 |
| Chain | Residue |
| E | GLU126 |
| E | ASP128 |
| E | ASP137 |
| E | HIS142 |
| E | HOH426 |
| E | HOH428 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ABU E 303 |
| Chain | Residue |
| E | PRO205 |
| E | GLU206 |
| E | TRP207 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA F 301 |
| Chain | Residue |
| F | ASP128 |
| F | TYR130 |
| F | ASN132 |
| F | ASP137 |
| F | HOH411 |
| F | HOH426 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 302 |
| Chain | Residue |
| F | GLU126 |
| F | ASP128 |
| F | ASP137 |
| F | HIS142 |
| F | HOH415 |
| F | HOH430 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL F 303 |
| Chain | Residue |
| F | HOH428 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA G 301 |
| Chain | Residue |
| G | ASP128 |
| G | TYR130 |
| G | ASN132 |
| G | ASP137 |
| G | HOH431 |
| G | HOH434 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN G 302 |
| Chain | Residue |
| G | GLU126 |
| G | ASP128 |
| G | ASP137 |
| G | HIS142 |
| G | HOH432 |
| G | HOH433 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA H 301 |
| Chain | Residue |
| H | ASP128 |
| H | TYR130 |
| H | ASN132 |
| H | ASP137 |
| H | HOH406 |
| H | HOH411 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN H 302 |
| Chain | Residue |
| H | GLU126 |
| H | ASP128 |
| H | ASP137 |
| H | HIS142 |
| H | HOH433 |
| site_id | CC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ABU H 303 |
| Chain | Residue |
| E | VAL7 |
| E | ASN17 |
| H | GLU2 |
| H | GLU3 |
| H | THR4 |
| H | ILE57 |
| H | ASN58 |
| H | TRP207 |
| H | SER235 |
| H | HOH404 |
| H | HOH414 |
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 |
| F | VAL134-TYR140 | |
| E | VAL134-TYR140 |
| site_id | PS00307 |
| Number of Residues | 7 |
| Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT |
| Chain | Residue | Details |
| A | VAL123-THR129 | |
| F | VAL123-THR129 | |
| E | VAL123-THR129 | |
| B | VAL123-THR129 |
| site_id | PS00308 |
| Number of Residues | 10 |
| Details | LECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVSIGFS |
| Chain | Residue | Details |
| A | LEU204-SER213 | |
| F | LEU204-SER213 | |
| E | LEU204-SER213 | |
| B | 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 |
| F | ASP88 | |
| H | ASP88 | |
| H | GLY106 | |
| H | GLU126 | |
| H | ASP128 | |
| H | ASN132 | |
| H | ASP137 | |
| H | HIS142 | |
| H | GLY217 | |
| H | ALA218 | |
| F | GLY106 | |
| F | GLU126 | |
| F | ASP128 | |
| F | ASN132 | |
| F | ASP137 | |
| F | HIS142 | |
| F | GLY217 | |
| F | 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 |
| E | GLU126 | |
| G | ASN132 | |
| G | ASP137 | |
| G | HIS142 | |
| E | ASP128 | |
| E | TYR130 | |
| E | ASN132 | |
| E | ASP137 | |
| E | HIS142 | |
| G | GLU126 | |
| G | ASP128 | |
| G | TYR130 |
