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7CL1

Human SIRT6 in complex with allosteric activator MDL-801 (3.2A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003684molecular_functiondamaged DNA binding
A0003714molecular_functiontranscription corepressor activity
A0003723molecular_functionRNA binding
A0003950molecular_functionNAD+ ADP-ribosyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005721cellular_componentpericentric heterochromatin
A0005730cellular_componentnucleolus
A0005783cellular_componentendoplasmic reticulum
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006302biological_processdouble-strand break repair
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006476biological_processprotein deacetylation
A0008270molecular_functionzinc ion binding
A0008285biological_processnegative regulation of cell population proliferation
A0008340biological_processdetermination of adult lifespan
A0009411biological_processresponse to UV
A0010526biological_processretrotransposon silencing
A0010569biological_processregulation of double-strand break repair via homologous recombination
A0016746molecular_functionacyltransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0019216biological_processregulation of lipid metabolic process
A0031490molecular_functionchromatin DNA binding
A0031491molecular_functionnucleosome binding
A0031508biological_processpericentric heterochromatin formation
A0031509biological_processsubtelomeric heterochromatin formation
A0031648biological_processprotein destabilization
A0032024biological_processpositive regulation of insulin secretion
A0032206biological_processpositive regulation of telomere maintenance
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032922biological_processcircadian regulation of gene expression
A0034244biological_processnegative regulation of transcription elongation by RNA polymerase II
A0034979molecular_functionNAD-dependent protein lysine deacetylase activity
A0035861cellular_componentsite of double-strand break
A0042181biological_processketone biosynthetic process
A0042308biological_processnegative regulation of protein import into nucleus
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0042803molecular_functionprotein homodimerization activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0043687biological_processpost-translational protein modification
A0045600biological_processpositive regulation of fat cell differentiation
A0045721biological_processnegative regulation of gluconeogenesis
A0045814biological_processnegative regulation of gene expression, epigenetic
A0045820biological_processnegative regulation of glycolytic process
A0045892biological_processnegative regulation of DNA-templated transcription
A0046325biological_processnegative regulation of glucose import
A0046827biological_processpositive regulation of protein export from nucleus
A0046872molecular_functionmetal ion binding
A0046969molecular_functionNAD-dependent histone H3K9 deacetylase activity
A0048146biological_processpositive regulation of fibroblast proliferation
A0050708biological_processregulation of protein secretion
A0050994biological_processregulation of lipid catabolic process
A0051697biological_processprotein delipidation
A0055007biological_processcardiac muscle cell differentiation
A0070403molecular_functionNAD+ binding
A0090734cellular_componentsite of DNA damage
A0097372molecular_functionNAD-dependent histone H3K18 deacetylase activity
A0099115cellular_componentchromosome, subtelomeric region
A0106222molecular_functionlncRNA binding
A0106274molecular_functionNAD+-protein-arginine ADP-ribosyltransferase activity
A0120162biological_processpositive regulation of cold-induced thermogenesis
A0120186biological_processnegative regulation of protein localization to chromatin
A0120187biological_processpositive regulation of protein localization to chromatin
A0140612molecular_functionDNA damage sensor activity
A0140765molecular_functionNAD-dependent histone H3K56 deacetylase activity
A0140773molecular_functionNAD-dependent protein demyristoylase activity
A0140774molecular_functionNAD-dependent protein depalmitoylase activity
A0140804molecular_functionNAD+- protein-lysine ADP-ribosyltransferase activity
A0140861biological_processDNA repair-dependent chromatin remodeling
A1902459biological_processpositive regulation of stem cell population maintenance
A1902732biological_processpositive regulation of chondrocyte proliferation
A1903076biological_processregulation of protein localization to plasma membrane
A1904841molecular_functionTORC2 complex binding
A1905555biological_processpositive regulation of blood vessel branching
A1905564biological_processpositive regulation of vascular endothelial cell proliferation
A1990166biological_processprotein localization to site of double-strand break
A1990404molecular_functionNAD+-protein ADP-ribosyltransferase activity
A2000648biological_processpositive regulation of stem cell proliferation
A2000738biological_processpositive regulation of stem cell differentiation
A2000773biological_processnegative regulation of cellular senescence
A2000781biological_processpositive regulation of double-strand break repair
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:18337721, ECO:0000305|PubMed:23552949, ECO:0000305|PubMed:23892288, ECO:0000305|PubMed:27322069, ECO:0000305|PubMed:28406396
ChainResidueDetails
AHIS131

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:21362626, ECO:0007744|PDB:3K35, ECO:0007744|PDB:3ZG6
ChainResidueDetails
AALA51

site_idSWS_FT_FI3
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:23552949, ECO:0000305|PubMed:21362626, ECO:0007744|PDB:3K35, ECO:0007744|PDB:3ZG6
ChainResidueDetails
ATHR55
AGLN240
AVAL256
APHE62
AARG63
ATRP69
AGLN111
AHIS131
AGLY212
ASER214
AASN238

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:21362626, ECO:0000269|PubMed:23552949, ECO:0000269|PubMed:27990725, ECO:0007744|PDB:3K35, ECO:0007744|PDB:3PKI, ECO:0007744|PDB:3PKJ, ECO:0007744|PDB:3ZG6, ECO:0007744|PDB:5MF6, ECO:0007744|PDB:5MFP, ECO:0007744|PDB:5MFZ, ECO:0007744|PDB:5MGN
ChainResidueDetails
ACYS139
ACYS142
ACYS164
ACYS175

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Formation of an covalent adduct with nitro-fatty acid activators => ECO:0000269|PubMed:33122195
ChainResidueDetails
ACYS16

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER0

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK8 => ECO:0000269|PubMed:27568560, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER8

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:32538779
ChainResidueDetails
ALYS31

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR292

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER301

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER328

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:24043303
ChainResidueDetails
ALYS168

222624

PDB entries from 2024-07-17

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