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5YH3

The structure of hFam20C and hFam20A complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001934biological_processpositive regulation of protein phosphorylation
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0031214biological_processbiomineral tissue development
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044691biological_processtooth eruption
A0055074biological_processcalcium ion homeostasis
A0070062cellular_componentextracellular exosome
A0070166biological_processenamel mineralization
B0001934biological_processpositive regulation of protein phosphorylation
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0031214biological_processbiomineral tissue development
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044691biological_processtooth eruption
B0055074biological_processcalcium ion homeostasis
B0070062cellular_componentextracellular exosome
B0070166biological_processenamel mineralization
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ATP A 701
ChainResidue
ATYR125
ASER346
ALEU347
AARG352
ALEU429
AASP430
CLYS347
ALYS129
ALYS233
AMET235
APRO279
ASER341
AALA342
APHE343
ALEU344

site_idAC2
Number of Residues13
Detailsbinding site for residue ATP A 702
ChainResidue
ALYS129
AARG132
AARG136
ATYR140
AGLN143
ASER195
AASP197
ALYS203
ALYS297
AASN298
AGLU299
CLYS347
CARG351

site_idAC3
Number of Residues12
Detailsbinding site for residue ATP B 701
ChainResidue
BTYR125
BLYS129
BLYS233
BMET235
BPRO279
BSER341
BALA342
BLEU344
BSER346
BLEU347
BARG352
BATP702

site_idAC4
Number of Residues11
Detailsbinding site for residue ATP B 702
ChainResidue
BLYS129
BARG132
BARG136
BTYR140
BGLN143
BSER195
BASP197
BLYS203
BARG227
BLYS297
BATP701

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues211
DetailsRegion: {"description":"Kinase domain","evidences":[{"source":"PubMed","id":"22582013","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"23754375","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9XTW2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22582013","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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