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1KPF

PKCI-SUBSTRATE ANALOG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005080molecular_functionprotein kinase C binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006355biological_processregulation of DNA-templated transcription
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0008234molecular_functioncysteine-type peptidase activity
A0009154biological_processpurine ribonucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016926biological_processprotein desumoylation
A0016929molecular_functiondeSUMOylase activity
A0043530molecular_functionadenosine 5'-monophosphoramidase activity
A0050850biological_processpositive regulation of calcium-mediated signaling
A0070062cellular_componentextracellular exosome
A0072332biological_processintrinsic apoptotic signaling pathway by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AMP A 200
ChainResidue
AILE44
ASER45
ALEU53
AASN99
AGLY105
AGLN106
ASER107
AVAL108
AHIS112
AHIS114
AHOH203
AHOH209
AHOH214
AHOH219
AHOH333
APHE19
ALYS25
AGLU34
AHIS42
AASP43

site_idAVE
Number of Residues1
DetailsACTIVE SITE HISTIDINE RESPONSIBLE FOR FORMING THE TRANSIENT NUCLEOTIDYL PHOSPHOHISTIDYL ENZYME INTERMEDIATE DURING CATALYSIS.
ChainResidue
AHIS112

site_idHNE
Number of Residues3
DetailsHISTIDINE TRIAD FOR WHICH THIS FAMILY WAS NAMED.
ChainResidue
AHIS51
AHIS112
AHIS114

Functional Information from PROSITE/UniProt
site_idPS00892
Number of Residues19
DetailsHIT_1 HIT domain signature. NegsdGgQsVyHVHLHVLG
ChainResidueDetails
AASN99-GLY117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:9323207
ChainResidueDetails
ALEU113

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22869114, ECO:0007744|PDB:3TW2
ChainResidueDetails
AILE44
AGLU100
AGLN106
ALEU113

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AASP3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AILE22
AILE31

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70349
ChainResidueDetails
APRO46
ALEU73

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 5fit
ChainResidueDetails
AHIS112
AASN99
AHIS110

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PDB entries from 2024-10-09

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