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8WS0

Crystal structure of human NEK7 S195D mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000922cellular_componentspindle pole
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005815cellular_componentmicrotubule organizing center
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006468biological_processprotein phosphorylation
A0007346biological_processregulation of mitotic cell cycle
A0009306biological_processprotein secretion
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0032206biological_processpositive regulation of telomere maintenance
A0032731biological_processpositive regulation of interleukin-1 beta production
A0032741biological_processpositive regulation of interleukin-18 production
A0033044biological_processregulation of chromosome organization
A0035655biological_processinterleukin-18-mediated signaling pathway
A0035865biological_processcellular response to potassium ion
A0044546biological_processNLRP3 inflammasome complex assembly
A0046872molecular_functionmetal ion binding
A0050729biological_processpositive regulation of inflammatory response
A0051225biological_processspindle assembly
A0051604biological_processprotein maturation
A0070269biological_processpyroptotic inflammatory response
A0070498biological_processinterleukin-1-mediated signaling pathway
A0106310molecular_functionprotein serine kinase activity
A0140677molecular_functionmolecular function activator activity
A1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
B0000166molecular_functionnucleotide binding
B0000922cellular_componentspindle pole
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005815cellular_componentmicrotubule organizing center
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006468biological_processprotein phosphorylation
B0007346biological_processregulation of mitotic cell cycle
B0009306biological_processprotein secretion
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0032206biological_processpositive regulation of telomere maintenance
B0032731biological_processpositive regulation of interleukin-1 beta production
B0032741biological_processpositive regulation of interleukin-18 production
B0033044biological_processregulation of chromosome organization
B0035655biological_processinterleukin-18-mediated signaling pathway
B0035865biological_processcellular response to potassium ion
B0044546biological_processNLRP3 inflammasome complex assembly
B0046872molecular_functionmetal ion binding
B0050729biological_processpositive regulation of inflammatory response
B0051225biological_processspindle assembly
B0051604biological_processprotein maturation
B0070269biological_processpyroptotic inflammatory response
B0070498biological_processinterleukin-1-mediated signaling pathway
B0106310molecular_functionprotein serine kinase activity
B0140677molecular_functionmolecular function activator activity
B1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGQFSEVYrAaclldgvp..........VALK
ChainResidueDetails
AILE40-LYS63

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VmHrDIKpaNVFI
ChainResidueDetails
AVAL157-ILE169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP161
BASP161

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:19941817, ECO:0007744|PDB:2WQN
ChainResidueDetails
AILE40
ALYS63
BILE40
BLYS63

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Autoinhibitory => ECO:0000269|PubMed:19941817
ChainResidueDetails
ATYR97
BTYR97

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER5
BSER5

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by NEK9 => ECO:0000269|PubMed:12840024, ECO:0000269|PubMed:26522158
ChainResidueDetails
AASP195
BASP195

237735

PDB entries from 2025-06-18

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