3IFK
Crystal Structure Of Calcium-Saturated Calmodulin N-terminal Domain Fragment, Residues 1-90
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 91 |
Chain | Residue |
A | ASP20 |
A | ASP22 |
A | ASP24 |
A | THR26 |
A | GLU31 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 92 |
Chain | Residue |
A | GLU67 |
A | ASP56 |
A | ASP58 |
A | ASN60 |
A | THR62 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 91 |
Chain | Residue |
B | ASP20 |
B | ASP22 |
B | ASP24 |
B | THR26 |
B | GLU31 |
B | HOH115 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 92 |
Chain | Residue |
B | ASP56 |
B | ASP58 |
B | ASN60 |
B | THR62 |
B | GLU67 |
B | HOH103 |
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
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 |
A | ASP20 | |
B | GLU31 | |
A | ASP22 | |
A | ASP24 | |
A | THR26 | |
A | GLU31 | |
B | ASP20 | |
B | ASP22 | |
B | ASP24 | |
B | THR26 |
Chain | Residue | Details |
A | ASP56 | |
B | GLU67 | |
A | ASP58 | |
A | ASN60 | |
A | THR62 | |
A | GLU67 | |
B | ASP56 | |
B | ASP58 | |
B | ASN60 | |
B | THR62 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS21 | |
B | LYS21 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717 |
Chain | Residue | Details |
A | THR44 | |
B | THR44 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | SER81 | |
B | SER81 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 |
Chain | Residue | Details |
A | LYS21 | |
B | LYS21 |