3EVU
Crystal structure of Calcium bound dimeric GCAMP2
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 505 |
Chain | Residue |
A | ASP396 |
A | ASP398 |
A | ASN400 |
A | TYR402 |
A | GLU407 |
A | HOH590 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 506 |
Chain | Residue |
A | GLN438 |
A | GLU443 |
A | HOH537 |
A | ASP432 |
A | ASP434 |
A | ASP436 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 507 |
Chain | Residue |
A | ASP359 |
A | ASP361 |
A | ASN363 |
A | THR365 |
A | GLU370 |
A | HOH608 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 508 |
Chain | Residue |
A | ASP323 |
A | ASP325 |
A | ASP327 |
A | THR329 |
A | GLU334 |
A | HOH545 |
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 | ASP325-THR337 | |
A | ASP361-THR373 | |
A | ASP398-HIS410 | |
A | ASP434-GLN446 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:12176732 |
Chain | Residue | Details |
A | ASN72 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
A | VAL226 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
A | CRO224 | |
A | GLN227 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
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 | ASP323 | |
A | ASP325 | |
A | ASP327 | |
A | THR329 | |
A | GLU334 |
Chain | Residue | Details |
A | ASP359 | |
A | ASP361 | |
A | ASN363 | |
A | THR365 | |
A | GLU370 |
site_id | SWS_FT_FI6 |
Number of Residues | 5 |
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 |
A | ASP396 | |
A | ASP398 | |
A | ASN400 | |
A | TYR402 | |
A | GLU407 |
site_id | SWS_FT_FI7 |
Number of Residues | 5 |
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 |
A | ASP432 | |
A | ASP434 | |
A | ASP436 | |
A | GLN438 | |
A | GLU443 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS324 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717 |
Chain | Residue | Details |
A | THR347 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | SER384 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS397 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | TYR402 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER404 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | THR413 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | LYS418 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23 |
Chain | Residue | Details |
A | TYR441 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157 |
Chain | Residue | Details |
A | LYS324 |