3SJQ
Crystal structure of a small conductance potassium channel splice variant complexed with calcium-calmodulin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
A | 0000922 | cellular_component | spindle pole |
A | 0001975 | biological_process | response to amphetamine |
A | 0002027 | biological_process | regulation of heart rate |
A | 0005246 | molecular_function | calcium channel regulator activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005513 | biological_process | detection of calcium ion |
A | 0005515 | molecular_function | protein binding |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005813 | cellular_component | centrosome |
A | 0005819 | cellular_component | spindle |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005876 | cellular_component | spindle microtubule |
A | 0005929 | cellular_component | cilium |
A | 0008076 | cellular_component | voltage-gated potassium channel complex |
A | 0008179 | molecular_function | adenylate cyclase binding |
A | 0010856 | molecular_function | adenylate cyclase activator activity |
A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
A | 0016020 | cellular_component | membrane |
A | 0016240 | biological_process | autophagosome membrane docking |
A | 0019855 | molecular_function | calcium channel inhibitor activity |
A | 0019901 | molecular_function | protein kinase binding |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0030017 | cellular_component | sarcomere |
A | 0030235 | molecular_function | nitric-oxide synthase regulator activity |
A | 0030426 | cellular_component | growth cone |
A | 0030672 | cellular_component | synaptic vesicle membrane |
A | 0031432 | molecular_function | titin binding |
A | 0031514 | cellular_component | motile cilium |
A | 0031800 | molecular_function | type 3 metabotropic glutamate receptor binding |
A | 0031966 | cellular_component | mitochondrial membrane |
A | 0031982 | cellular_component | vesicle |
A | 0032465 | biological_process | regulation of cytokinesis |
A | 0032991 | cellular_component | protein-containing complex |
A | 0034704 | cellular_component | calcium channel complex |
A | 0035458 | biological_process | cellular response to interferon-beta |
A | 0042995 | cellular_component | cell projection |
A | 0043209 | cellular_component | myelin sheath |
A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
A | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
A | 0044305 | cellular_component | calyx of Held |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
A | 0046872 | molecular_function | metal ion binding |
A | 0048306 | molecular_function | calcium-dependent protein binding |
A | 0050848 | biological_process | regulation of calcium-mediated signaling |
A | 0050998 | molecular_function | nitric-oxide synthase binding |
A | 0051592 | biological_process | response to calcium ion |
A | 0055117 | biological_process | regulation of cardiac muscle contraction |
A | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
A | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
A | 0071346 | biological_process | cellular response to type II interferon |
A | 0072542 | molecular_function | protein phosphatase activator activity |
A | 0090150 | biological_process | establishment of protein localization to membrane |
A | 0090151 | biological_process | establishment of protein localization to mitochondrial membrane |
A | 0097225 | cellular_component | sperm midpiece |
A | 0097720 | biological_process | calcineurin-mediated signaling |
A | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0099524 | cellular_component | postsynaptic cytosol |
A | 0140056 | biological_process | organelle localization by membrane tethering |
A | 0140238 | biological_process | presynaptic endocytosis |
A | 0141110 | molecular_function | transporter inhibitor activity |
A | 1900242 | biological_process | regulation of synaptic vesicle endocytosis |
A | 1902494 | cellular_component | catalytic complex |
A | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
A | 2000300 | biological_process | regulation of synaptic vesicle exocytosis |
B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
B | 0000922 | cellular_component | spindle pole |
B | 0001975 | biological_process | response to amphetamine |
B | 0002027 | biological_process | regulation of heart rate |
B | 0005246 | molecular_function | calcium channel regulator activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005513 | biological_process | detection of calcium ion |
B | 0005515 | molecular_function | protein binding |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005813 | cellular_component | centrosome |
B | 0005819 | cellular_component | spindle |
B | 0005829 | cellular_component | cytosol |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005876 | cellular_component | spindle microtubule |
B | 0005929 | cellular_component | cilium |
B | 0008076 | cellular_component | voltage-gated potassium channel complex |
B | 0008179 | molecular_function | adenylate cyclase binding |
B | 0010856 | molecular_function | adenylate cyclase activator activity |
B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
B | 0016020 | cellular_component | membrane |
B | 0016240 | biological_process | autophagosome membrane docking |
B | 0019855 | molecular_function | calcium channel inhibitor activity |
B | 0019901 | molecular_function | protein kinase binding |
B | 0019904 | molecular_function | protein domain specific binding |
B | 0030017 | cellular_component | sarcomere |
B | 0030235 | molecular_function | nitric-oxide synthase regulator activity |
B | 0030426 | cellular_component | growth cone |
B | 0030672 | cellular_component | synaptic vesicle membrane |
B | 0031432 | molecular_function | titin binding |
B | 0031514 | cellular_component | motile cilium |
B | 0031800 | molecular_function | type 3 metabotropic glutamate receptor binding |
B | 0031966 | cellular_component | mitochondrial membrane |
B | 0031982 | cellular_component | vesicle |
B | 0032465 | biological_process | regulation of cytokinesis |
B | 0032991 | cellular_component | protein-containing complex |
B | 0034704 | cellular_component | calcium channel complex |
B | 0035458 | biological_process | cellular response to interferon-beta |
B | 0042995 | cellular_component | cell projection |
B | 0043209 | cellular_component | myelin sheath |
B | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
B | 0043548 | molecular_function | phosphatidylinositol 3-kinase binding |
B | 0044305 | cellular_component | calyx of Held |
B | 0044325 | molecular_function | transmembrane transporter binding |
B | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
B | 0046872 | molecular_function | metal ion binding |
B | 0048306 | molecular_function | calcium-dependent protein binding |
B | 0050848 | biological_process | regulation of calcium-mediated signaling |
B | 0050998 | molecular_function | nitric-oxide synthase binding |
B | 0051592 | biological_process | response to calcium ion |
B | 0055117 | biological_process | regulation of cardiac muscle contraction |
B | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
B | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
B | 0071346 | biological_process | cellular response to type II interferon |
B | 0072542 | molecular_function | protein phosphatase activator activity |
B | 0090150 | biological_process | establishment of protein localization to membrane |
B | 0090151 | biological_process | establishment of protein localization to mitochondrial membrane |
B | 0097225 | cellular_component | sperm midpiece |
B | 0097720 | biological_process | calcineurin-mediated signaling |
B | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
B | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
B | 0099523 | cellular_component | presynaptic cytosol |
B | 0099524 | cellular_component | postsynaptic cytosol |
B | 0140056 | biological_process | organelle localization by membrane tethering |
B | 0140238 | biological_process | presynaptic endocytosis |
B | 0141110 | molecular_function | transporter inhibitor activity |
B | 1900242 | biological_process | regulation of synaptic vesicle endocytosis |
B | 1902494 | cellular_component | catalytic complex |
B | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
B | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
B | 2000300 | biological_process | regulation of synaptic vesicle exocytosis |
C | 0005516 | molecular_function | calmodulin binding |
C | 0006813 | biological_process | potassium ion transport |
C | 0015269 | molecular_function | calcium-activated potassium channel activity |
C | 0016020 | cellular_component | membrane |
C | 0016286 | molecular_function | small conductance calcium-activated potassium channel activity |
D | 0005516 | molecular_function | calmodulin binding |
D | 0006813 | biological_process | potassium ion transport |
D | 0015269 | molecular_function | calcium-activated potassium channel activity |
D | 0016020 | cellular_component | membrane |
D | 0016286 | molecular_function | small conductance calcium-activated potassium channel activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1001 |
Chain | Residue |
A | ASP20 |
A | ASP22 |
A | ASP24 |
A | THR26 |
A | GLU31 |
A | HOH155 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1002 |
Chain | Residue |
A | THR62 |
A | GLU67 |
A | HOH156 |
A | ASP56 |
A | ASP58 |
A | ASN60 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1003 |
Chain | Residue |
A | ASP93 |
A | ASP95 |
A | ASN97 |
A | TYR99 |
A | GLU104 |
A | HOH157 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1004 |
Chain | Residue |
A | ASP129 |
A | ASP131 |
A | ASP133 |
A | GLN135 |
A | GLU140 |
A | HOH158 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PHU A 2001 |
Chain | Residue |
A | PHE19 |
A | LEU32 |
A | MET51 |
A | GLU54 |
A | VAL55 |
A | ILE63 |
A | PHE68 |
A | MET71 |
C | ALA480 |
C | LEU483 |
C | VAL484 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 149 |
Chain | Residue |
A | ASN97 |
A | TYR99 |
A | HOH165 |
B | LYS21 |
B | HOH154 |
B | HOH258 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 150 |
Chain | Residue |
A | LEU18 |
A | LYS21 |
A | SER38 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 151 |
Chain | Residue |
A | LYS21 |
A | HOH163 |
A | HOH170 |
A | HOH255 |
B | ASN97 |
B | TYR99 |
B | HOH166 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 152 |
Chain | Residue |
A | ASP64 |
A | HOH277 |
B | THR79 |
D | ASN481 |
D | VAL484 |
D | ASP485 |
D | LYS488 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 153 |
Chain | Residue |
A | THR34 |
A | ARG37 |
A | HOH289 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 154 |
Chain | Residue |
A | ARG106 |
A | HIS107 |
A | THR110 |
A | HOH312 |
C | HOH159 |
C | ARG450 |
C | ARG454 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1001 |
Chain | Residue |
B | ASP20 |
B | ASP22 |
B | ASP24 |
B | THR26 |
B | GLU31 |
B | HOH153 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1002 |
Chain | Residue |
B | ASP56 |
B | ASP58 |
B | ASN60 |
B | THR62 |
B | GLU67 |
B | HOH157 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1003 |
Chain | Residue |
B | ASP93 |
B | ASP95 |
B | ASN97 |
B | TYR99 |
B | GLU104 |
B | HOH159 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 1004 |
Chain | Residue |
B | ASP129 |
B | ASP131 |
B | ASP133 |
B | GLN135 |
B | GLU140 |
B | HOH160 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PHU B 2001 |
Chain | Residue |
B | MET71 |
D | ALA480 |
D | LEU483 |
D | VAL484 |
B | PHE19 |
B | LEU32 |
B | MET51 |
B | GLU54 |
B | VAL55 |
B | ILE63 |
B | PHE68 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 149 |
Chain | Residue |
B | LEU18 |
B | LYS21 |
B | SER38 |
B | LEU39 |
B | HOH253 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 150 |
Chain | Residue |
B | THR34 |
B | ARG37 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 151 |
Chain | Residue |
B | ALA102 |
B | ARG106 |
B | HOH195 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 152 |
Chain | Residue |
B | GLU123 |
B | ARG126 |
C | ARG467 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 5 |
Chain | Residue |
C | LYS436 |
C | ASN437 |
C | LYS448 |
C | HIS452 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PHU C 2 |
Chain | Residue |
B | ALA57 |
B | GLU67 |
B | THR70 |
B | HOH196 |
C | LEU486 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL D 2 |
Chain | Residue |
D | LYS436 |
D | ASN437 |
D | LYS448 |
D | HIS452 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 3 |
Chain | Residue |
B | ARG106 |
B | HIS107 |
D | HOH281 |
D | HOH308 |
D | ARG450 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 8 |
Chain | Residue |
A | ARG126 |
D | ARG467 |
D | LYS470 |
D | ARG474 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PHU D 1 |
Chain | Residue |
A | ALA57 |
A | THR70 |
D | THR482 |
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 |
A | ASP20-LEU32 | |
A | ASP56-PHE68 | |
A | ASP93-LEU105 | |
A | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 70 |
Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 70 |
Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 70 |
Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11323678","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23109337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3145979","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G4Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HQW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G27","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G28","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J9Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QNH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11323678","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23109337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3145979","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G4Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HQW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3B32","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EKH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G27","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G28","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4J9Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QNH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23109337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3145979","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HQW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EKH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RJD","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23109337","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3145979","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HQW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YGG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BXL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EKH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3EVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SG7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WLD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EHQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RJD","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"201628","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2007","submissionDatabase":"UniProtKB","authors":["Lubec G.","Chen W.-Q."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"PubMed","id":"12392717","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |