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2XNM

Structure of NEK2 bound to CCT

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE WGZ A 1280
ChainResidue
AILE14
AALA145
APHE148
AGLY158
AASP159
ALEU162
ALEU166
AHOH2245
AGLY15
ACYS22
ALYS37
AGLU87
ATYR88
ACYS89
AASP93
ASER96

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1281
ChainResidue
ALEU11
ALYS152
AGLN153
AHOH2241
AHOH2246
AHOH2247

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1282
ChainResidue
AILE247
AGLU264
AASN268

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1283
ChainResidue
AASP242
AGLU243
AGLU246
AHIS277
AHIS279
AHOH2249

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1284
ChainResidue
ATYR238
AARG239
ASER241
AHOH2250
AHOH2251
AHOH2252

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1285
ChainResidue
ATYR12
AARG115
AGLN153

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1286
ChainResidue
AARG234
AARG235
ATYR238
ALEU266
AHOH2230
AHOH2254
AHOH2255

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1287
ChainResidue
ATYR181
ATYR182
AGLU208
APRO214
AHOH2257
AHOH2258

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1288
ChainResidue
AGLU195
ALYS196
ASER261
AVAL262
AHOH2223
AHOH2259

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1290
ChainResidue
AGLU110
AARG239

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1292
ChainResidue
AASN154
AHIS277
AHOH2150

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 1291
ChainResidue
AHIS128
AARG130
ATYR193
AASN194
AGLU195
AASP198
AHOH2260

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNVFL
ChainResidueDetails
AVAL137-LEU149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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