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2XKC

Structure of Nek2 bound to aminopyrazine compound 14

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 Residues11
DetailsBINDING SITE FOR RESIDUE 4VQ A 1280
ChainResidue
AILE14
APHE148
AGLY158
ACYS22
AVAL35
ALYS37
AMET86
AGLU87
ACYS89
AGLU90
AGLY92

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1282
ChainResidue
AARG105

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1283
ChainResidue
AGLU110
AARG239

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1284
ChainResidue
AARG235

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP141

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE14

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS37

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000305|PubMed:17197699
ChainResidueDetails
ATHR170

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000305|PubMed:17197699, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER171

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17197699
ChainResidueDetails
ATHR175
ATHR179

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER184

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:17197699
ChainResidueDetails
ASER241

218853

PDB entries from 2024-04-24

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