9EIO
Cryo-EM structure of the mutant KCa2.2_F244S channel
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 |
E | ASP20-LEU32 | |
E | ASP56-PHE68 | |
E | ASP93-LEU105 | |
E | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:11323678, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH |
Chain | Residue | Details |
E | ASP20 | |
F | GLU31 | |
G | ASP20 | |
G | ASP22 | |
G | ASP24 | |
G | THR26 | |
G | GLU31 | |
H | ASP20 | |
H | ASP22 | |
H | ASP24 | |
H | THR26 | |
E | ASP22 | |
H | GLU31 | |
E | ASP24 | |
E | THR26 | |
E | GLU31 | |
F | ASP20 | |
F | ASP22 | |
F | ASP24 | |
F | THR26 |
Chain | Residue | Details |
E | ASP56 | |
F | GLU67 | |
G | ASP56 | |
G | ASP58 | |
G | ASN60 | |
G | THR62 | |
G | GLU67 | |
H | ASP56 | |
H | ASP58 | |
H | ASN60 | |
H | THR62 | |
E | ASP58 | |
H | GLU67 | |
E | ASN60 | |
E | THR62 | |
E | GLU67 | |
F | ASP56 | |
F | ASP58 | |
F | ASN60 | |
F | THR62 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
Chain | Residue | Details |
E | ASP93 | |
F | GLU104 | |
G | ASP93 | |
G | ASP95 | |
G | ASN97 | |
G | TYR99 | |
G | GLU104 | |
H | ASP93 | |
H | ASP95 | |
H | ASN97 | |
H | TYR99 | |
E | ASP95 | |
H | GLU104 | |
E | ASN97 | |
E | TYR99 | |
E | GLU104 | |
F | ASP93 | |
F | ASP95 | |
F | ASN97 | |
F | TYR99 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD |
Chain | Residue | Details |
E | ASP129 | |
F | GLU140 | |
G | ASP129 | |
G | ASP131 | |
G | ASP133 | |
G | GLN135 | |
G | GLU140 | |
H | ASP129 | |
H | ASP131 | |
H | ASP133 | |
H | GLN135 | |
E | ASP131 | |
H | GLU140 | |
E | ASP133 | |
E | GLN135 | |
E | GLU140 | |
F | ASP129 | |
F | ASP131 | |
F | ASP133 | |
F | GLN135 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | LYS21 | |
F | LYS21 | |
G | LYS21 | |
H | LYS21 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717 |
Chain | Residue | Details |
E | THR44 | |
F | THR44 | |
G | THR44 | |
H | THR44 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | SER81 | |
F | SER81 | |
G | SER81 | |
H | SER81 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | LYS94 | |
F | LYS94 | |
G | LYS94 | |
H | LYS94 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
E | TYR99 | |
F | TYR99 | |
G | TYR99 | |
H | TYR99 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
E | SER101 | |
F | SER101 | |
G | SER101 | |
H | SER101 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | THR110 | |
F | THR110 | |
G | THR110 | |
H | THR110 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | LYS115 | |
F | LYS115 | |
G | LYS115 | |
H | LYS115 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
E | TYR138 | |
F | TYR138 | |
G | TYR138 | |
H | TYR138 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 |
Chain | Residue | Details |
E | LYS21 | |
F | LYS21 | |
G | LYS21 | |
H | LYS21 |