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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
A0009617biological_processresponse to bacterium
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
B0009617biological_processresponse to bacterium
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 Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:23754375
ChainResidueDetails
CASP458
DASP458
AASN287
AASN388
BASN70
BASN145
BASN287
BASN388

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9XTW2
ChainResidueDetails
CGLU306
CALA389
CGLU463
DGLN269
DLYS285
DGLU306
DALA389
DGLU463
CGLN269
CLYS285

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:22582013
ChainResidueDetails
CASP478
DASP478

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26091039
ChainResidueDetails
CASN335
DASN335

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26091039
ChainResidueDetails
CASN470
DASN470

219869

PDB entries from 2024-05-15

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