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4APC

Crystal Structure of Human NIMA-related Kinase 1 (NEK1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1285
ChainResidue
AMET80
AGLY145
AASP146
APHE147

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1286
ChainResidue
AGLN101

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1287
ChainResidue
AHIS120
AASN182
AVAL249

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1288
ChainResidue
AARG244
AASN242

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1285
ChainResidue
BHIS120
BASN182
BSER248
BVAL249

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1286
ChainResidue
BASN-5
BGLY74

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1287
ChainResidue
BASN242
BPRO243
BARG244

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSFGKAIlVkstedgrq..........YVIK
ChainResidueDetails
AILE10-LYS33

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDIKsqNIFL
ChainResidueDetails
AILE124-LEU136

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
AASP128
BASP128

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE10
ALYS33
BILE10
BLYS33

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR156
BTHR156

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250
ChainResidueDetails
AALA162
BALA162

223166

PDB entries from 2024-07-31

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