Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6XU4

Crystal structure of the genetically-encoded FGCaMP calcium indicator in its calcium-bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0001411cellular_componenthyphal tip
A0005509molecular_functioncalcium ion binding
A0005737cellular_componentcytoplasm
A0005823cellular_componentcentral plaque of spindle pole body
A0006091biological_processgeneration of precursor metabolites and energy
A0008218biological_processbioluminescence
A0009847biological_processspore germination
A0030234molecular_functionenzyme regulator activity
A0051286cellular_componentcell tip
A0051300biological_processspindle pole body organization
A0051726biological_processregulation of cell cycle
B0000226biological_processmicrotubule cytoskeleton organization
B0001411cellular_componenthyphal tip
B0005509molecular_functioncalcium ion binding
B0005737cellular_componentcytoplasm
B0005823cellular_componentcentral plaque of spindle pole body
B0006091biological_processgeneration of precursor metabolites and energy
B0008218biological_processbioluminescence
B0009847biological_processspore germination
B0030234molecular_functionenzyme regulator activity
B0051286cellular_componentcell tip
B0051300biological_processspindle pole body organization
B0051726biological_processregulation of cell cycle
E0000226biological_processmicrotubule cytoskeleton organization
E0001411cellular_componenthyphal tip
E0005509molecular_functioncalcium ion binding
E0005737cellular_componentcytoplasm
E0005823cellular_componentcentral plaque of spindle pole body
E0006091biological_processgeneration of precursor metabolites and energy
E0008218biological_processbioluminescence
E0009847biological_processspore germination
E0030234molecular_functionenzyme regulator activity
E0051286cellular_componentcell tip
E0051300biological_processspindle pole body organization
E0051726biological_processregulation of cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 501
ChainResidue
AASP323
AASP325
AASN327
ATHR329
AASP331
AGLU334

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 502
ChainResidue
APHE366
AGLU371
AASP360
AASP362
AASN364

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 503
ChainResidue
AASP287
AASP289
AASP291
AGLN293
AGLU298

site_idAC4
Number of Residues5
Detailsbinding site for residue CA A 504
ChainResidue
AASP396
AASP398
AASP400
AARG402
AGLU407

site_idAC5
Number of Residues5
Detailsbinding site for residue CA B 501
ChainResidue
BASP287
BASP289
BASP291
BGLN293
BGLU298

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 502
ChainResidue
BASP323
BASP325
BASN327
BTHR329
BASP331
BGLU334

site_idAC7
Number of Residues5
Detailsbinding site for residue CA B 503
ChainResidue
BASP360
BASP362
BASN364
BPHE366
BGLU371

site_idAC8
Number of Residues5
Detailsbinding site for residue CA B 504
ChainResidue
BASP396
BASP398
BASP400
BARG402
BGLU407

site_idAC9
Number of Residues5
Detailsbinding site for residue CA E 501
ChainResidue
EASP287
EASP289
EASP291
EGLN293
EGLU298

site_idAD1
Number of Residues6
Detailsbinding site for residue CA E 502
ChainResidue
EASP323
EASP325
EASN327
ETHR329
EASP331
EGLU334

site_idAD2
Number of Residues16
Detailsbinding site for Di-peptide LEU B 183 and CRO B 185
ChainResidue
BASN23
BILE41
BVAL77
BLEU94
BGLU96
BLEU163
BPHE165
BLEU179
BVAL180
BTHR181
BTHR182
BVAL187
BGLN188
BGLN213
BARG215
BASN240

site_idAD3
Number of Residues18
Detailsbinding site for Di-peptide CRO B 185 and VAL B 187
ChainResidue
BASN23
BILE41
BVAL77
BLEU94
BGLU96
BLEU161
BLEU163
BVAL180
BTHR181
BTHR182
BLEU183
BGLN188
BCYS189
BPHE190
BGLN213
BARG215
BLEU238
BASN240

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGQITtkEL
ChainResidueDetails
AASP289-THR301
AASP325-THR337
AASP362-HIS374
AASP398-GLN410

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

PDB statisticsPDBj update infoContact PDBjnumon