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2XNN

Structure of Nek2 bound to CCT242430

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 Residues12
DetailsBINDING SITE FOR RESIDUE 430 A 1280
ChainResidue
AILE14
AASN146
APHE148
AASP159
ACYS22
ALYS37
AGLU87
ATYR88
ACYS89
AGLY92
AASP93
AALA145

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1281
ChainResidue
AARG235

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1282
ChainResidue
AARG105

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1283
ChainResidue
APRO65
AASN154
AHIS277
AHOH2057

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1284
ChainResidue
ASER261
AVAL262

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1285
ChainResidue
ATYR181
ATYR182
AGLU208
APRO214
AHOH2109

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1286
ChainResidue
AILE247
AARG250
AGLU264
AASN268

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1287
ChainResidue
AGLY231
ALYS232
APHE233
ALEU272
AGLU273
AHIS274

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1288
ChainResidue
ALEU11
ALYS152
AGLN153
AHIS278

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1289
ChainResidue
AALA5
ATYR8
AVAL10
ATRP36
ATYR257
AHIS258

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1290
ChainResidue
APRO237
ATYR238
AARG239
AHOH2111

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 Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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