1Y0V
Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0008237 | molecular_function | metallopeptidase activity |
| E | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005576 | cellular_component | extracellular region |
| F | 0008237 | molecular_function | metallopeptidase activity |
| F | 0008294 | molecular_function | calcium- and calmodulin-responsive adenylate cyclase activity |
| F | 0046872 | molecular_function | metal ion binding |
| H | 0005102 | molecular_function | signaling receptor binding |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0016460 | cellular_component | myosin II complex |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005102 | molecular_function | signaling receptor binding |
| I | 0005509 | molecular_function | calcium ion binding |
| I | 0016460 | cellular_component | myosin II complex |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0005102 | molecular_function | signaling receptor binding |
| J | 0005509 | molecular_function | calcium ion binding |
| J | 0016460 | cellular_component | myosin II complex |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0005102 | molecular_function | signaling receptor binding |
| K | 0005509 | molecular_function | calcium ion binding |
| K | 0016460 | cellular_component | myosin II complex |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0005102 | molecular_function | signaling receptor binding |
| L | 0005509 | molecular_function | calcium ion binding |
| L | 0016460 | cellular_component | myosin II complex |
| L | 0046872 | molecular_function | metal ion binding |
| M | 0005102 | molecular_function | signaling receptor binding |
| M | 0005509 | molecular_function | calcium ion binding |
| M | 0016460 | cellular_component | myosin II complex |
| M | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 900 |
| Chain | Residue |
| A | ASP491 |
| A | ASP493 |
| A | HIS577 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | ASP491 |
| B | ASP493 |
| B | HIS577 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 902 |
| Chain | Residue |
| C | ASP491 |
| C | ASP493 |
| C | HIS577 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 903 |
| Chain | Residue |
| D | LYS346 |
| D | ASP491 |
| D | ASP493 |
| D | HIS577 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 904 |
| Chain | Residue |
| E | ASP491 |
| E | ASP493 |
| E | HIS577 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 905 |
| Chain | Residue |
| F | ASP491 |
| F | ASP493 |
| F | HIS577 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA H 701 |
| Chain | Residue |
| H | ASP20 |
| H | ASP22 |
| H | ASP24 |
| H | THR26 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 801 |
| Chain | Residue |
| H | ASP129 |
| H | ASP131 |
| H | ASP133 |
| H | GLN135 |
| H | GLU140 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 802 |
| Chain | Residue |
| H | ASP93 |
| H | ASP95 |
| H | ASN97 |
| H | TYR99 |
| H | GLU104 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA I 703 |
| Chain | Residue |
| I | ASP20 |
| I | ASP22 |
| I | ASP24 |
| I | THR26 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA I 803 |
| Chain | Residue |
| I | ASP129 |
| I | ASP131 |
| I | ASP133 |
| I | GLN135 |
| I | GLU140 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA I 804 |
| Chain | Residue |
| I | ASP93 |
| I | ASP95 |
| I | ASN97 |
| I | TYR99 |
| I | GLU104 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA J 705 |
| Chain | Residue |
| J | ASP20 |
| J | ASP22 |
| J | ASP24 |
| J | THR26 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA J 805 |
| Chain | Residue |
| J | ASP129 |
| J | ASP131 |
| J | ASP133 |
| J | GLN135 |
| J | GLU140 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA J 806 |
| Chain | Residue |
| J | ASP93 |
| J | ASP95 |
| J | ASN97 |
| J | TYR99 |
| J | GLU104 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA K 707 |
| Chain | Residue |
| K | ASP20 |
| K | ASP22 |
| K | ASP24 |
| K | THR26 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA K 807 |
| Chain | Residue |
| K | ASP129 |
| K | ASP131 |
| K | ASP133 |
| K | GLN135 |
| K | GLU140 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA K 808 |
| Chain | Residue |
| K | ASP93 |
| K | ASP95 |
| K | ASN97 |
| K | TYR99 |
| K | GLU104 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA L 709 |
| Chain | Residue |
| L | ASP20 |
| L | ASP22 |
| L | ASP24 |
| L | THR26 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA L 809 |
| Chain | Residue |
| L | ASP129 |
| L | ASP131 |
| L | ASP133 |
| L | GLN135 |
| L | GLU140 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA L 810 |
| Chain | Residue |
| L | ASP93 |
| L | ASP95 |
| L | ASN97 |
| L | TYR99 |
| L | GLU104 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA M 711 |
| Chain | Residue |
| M | ASP20 |
| M | ASP22 |
| M | ASP24 |
| M | THR26 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA M 811 |
| Chain | Residue |
| M | ASP129 |
| M | ASP131 |
| M | ASP133 |
| M | GLN135 |
| M | GLU140 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA M 812 |
| Chain | Residue |
| M | ASP95 |
| M | ASN97 |
| M | TYR99 |
| M | GLU104 |
| M | ASP93 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP A 901 |
| Chain | Residue |
| A | LYS346 |
| A | SER354 |
| A | LYS372 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP B 902 |
| Chain | Residue |
| B | LYS346 |
| B | SER354 |
| B | LYS372 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP C 903 |
| Chain | Residue |
| C | LYS346 |
| C | SER354 |
| C | LYS372 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP D 904 |
| Chain | Residue |
| D | LYS346 |
| D | SER354 |
| D | LYS372 |
| site_id | DC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP E 905 |
| Chain | Residue |
| E | LYS346 |
| E | SER354 |
| E | LYS372 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE POP F 906 |
| Chain | Residue |
| F | LYS346 |
| F | SER354 |
| F | LYS372 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
| Chain | Residue | Details |
| H | ASP20-LEU32 | |
| H | ASP56-PHE68 | |
| H | ASP93-LEU105 | |
| H | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448 |
| Chain | Residue | Details |
| H | LYS21 | |
| H | PHE68 | |
| L | PHE141 | |
| M | LYS21 | |
| M | GLY23 | |
| M | GLY25 | |
| M | ILE27 | |
| M | LEU32 | |
| M | ALA57 | |
| M | GLY59 | |
| M | GLY61 | |
| M | ILE63 | |
| H | LYS94 | |
| M | PHE68 | |
| M | LYS94 | |
| M | GLY96 | |
| M | GLY98 | |
| M | ILE100 | |
| M | LEU105 | |
| M | ILE130 | |
| M | GLY132 | |
| M | GLY134 | |
| M | VAL136 | |
| H | GLY96 | |
| M | PHE141 | |
| H | GLY98 | |
| H | ILE100 | |
| H | LEU105 | |
| H | ILE130 | |
| H | GLY132 | |
| H | GLY134 | |
| H | VAL136 | |
| H | GLY23 | |
| H | PHE141 | |
| I | LYS21 | |
| I | GLY23 | |
| I | GLY25 | |
| I | ILE27 | |
| I | LEU32 | |
| I | ALA57 | |
| I | GLY59 | |
| I | GLY61 | |
| I | ILE63 | |
| H | GLY25 | |
| I | PHE68 | |
| I | LYS94 | |
| I | GLY96 | |
| I | GLY98 | |
| I | ILE100 | |
| I | LEU105 | |
| I | ILE130 | |
| I | GLY132 | |
| I | GLY134 | |
| I | VAL136 | |
| H | ILE27 | |
| I | PHE141 | |
| J | LYS21 | |
| J | GLY23 | |
| J | GLY25 | |
| J | ILE27 | |
| J | LEU32 | |
| J | ALA57 | |
| J | GLY59 | |
| J | GLY61 | |
| J | ILE63 | |
| H | LEU32 | |
| J | PHE68 | |
| J | LYS94 | |
| J | GLY96 | |
| J | GLY98 | |
| J | ILE100 | |
| J | LEU105 | |
| J | ILE130 | |
| J | GLY132 | |
| J | GLY134 | |
| J | VAL136 | |
| H | ALA57 | |
| J | PHE141 | |
| K | LYS21 | |
| K | GLY23 | |
| K | GLY25 | |
| K | ILE27 | |
| K | LEU32 | |
| K | ALA57 | |
| K | GLY59 | |
| K | GLY61 | |
| K | ILE63 | |
| H | GLY59 | |
| K | PHE68 | |
| K | LYS94 | |
| K | GLY96 | |
| K | GLY98 | |
| K | ILE100 | |
| K | LEU105 | |
| K | ILE130 | |
| K | GLY132 | |
| K | GLY134 | |
| K | VAL136 | |
| H | GLY61 | |
| K | PHE141 | |
| L | LYS21 | |
| L | GLY23 | |
| L | GLY25 | |
| L | ILE27 | |
| L | LEU32 | |
| L | ALA57 | |
| L | GLY59 | |
| L | GLY61 | |
| L | ILE63 | |
| H | ILE63 | |
| L | PHE68 | |
| L | LYS94 | |
| L | GLY96 | |
| L | GLY98 | |
| L | ILE100 | |
| L | LEU105 | |
| L | ILE130 | |
| L | GLY132 | |
| L | GLY134 | |
| L | VAL136 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P0DP23 |
| Chain | Residue | Details |
| H | LEU116 | |
| D | ASP491 | |
| D | ASP493 | |
| D | HIS577 | |
| E | ASP491 | |
| E | ASP493 | |
| E | HIS577 | |
| F | ASP491 | |
| F | ASP493 | |
| F | HIS577 | |
| I | LEU116 | |
| J | LEU116 | |
| K | LEU116 | |
| L | LEU116 | |
| M | LEU116 | |
| C | ASP491 | |
| C | ASP493 | |
| C | HIS577 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15719022, ECO:0007744|PDB:1XFW |
| Chain | Residue | Details |
| A | THR548 | |
| B | THR548 | |
| C | THR548 | |
| D | THR548 | |
| E | THR548 | |
| F | THR548 |
