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6KAJ

Crystal structure of FKRP in complex with Ba ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0002162molecular_functiondystroglycan binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005791cellular_componentrough endoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0006486biological_processobsolete protein glycosylation
A0016740molecular_functiontransferase activity
A0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
A0035269biological_processprotein O-linked glycosylation via mannose
A0042383cellular_componentsarcolemma
A0042802molecular_functionidentical protein binding
A0043236molecular_functionlaminin binding
A0046872molecular_functionmetal ion binding
A0051262biological_processprotein tetramerization
A0098723cellular_componentskeletal muscle myofibril
B0000139cellular_componentGolgi membrane
B0002162molecular_functiondystroglycan binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005791cellular_componentrough endoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0006486biological_processobsolete protein glycosylation
B0016740molecular_functiontransferase activity
B0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
B0035269biological_processprotein O-linked glycosylation via mannose
B0042383cellular_componentsarcolemma
B0042802molecular_functionidentical protein binding
B0043236molecular_functionlaminin binding
B0046872molecular_functionmetal ion binding
B0051262biological_processprotein tetramerization
B0098723cellular_componentskeletal muscle myofibril
C0000139cellular_componentGolgi membrane
C0002162molecular_functiondystroglycan binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005737cellular_componentcytoplasm
C0005791cellular_componentrough endoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0006486biological_processobsolete protein glycosylation
C0016740molecular_functiontransferase activity
C0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
C0035269biological_processprotein O-linked glycosylation via mannose
C0042383cellular_componentsarcolemma
C0042802molecular_functionidentical protein binding
C0043236molecular_functionlaminin binding
C0046872molecular_functionmetal ion binding
C0051262biological_processprotein tetramerization
C0098723cellular_componentskeletal muscle myofibril
D0000139cellular_componentGolgi membrane
D0002162molecular_functiondystroglycan binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005791cellular_componentrough endoplasmic reticulum
D0005794cellular_componentGolgi apparatus
D0006486biological_processobsolete protein glycosylation
D0016740molecular_functiontransferase activity
D0016780molecular_functionphosphotransferase activity, for other substituted phosphate groups
D0035269biological_processprotein O-linked glycosylation via mannose
D0042383cellular_componentsarcolemma
D0042802molecular_functionidentical protein binding
D0043236molecular_functionlaminin binding
D0046872molecular_functionmetal ion binding
D0051262biological_processprotein tetramerization
D0098723cellular_componentskeletal muscle myofibril
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsRegion: {"description":"Zinc finger loop","evidences":[{"source":"PubMed","id":"31949166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KAJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31949166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KAJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31949166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KAJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KAM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31949166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KAL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21886772","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31949166","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6KAJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KAL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KAM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6KAN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6L7S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6L7T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6L7U","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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