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6CKI

Co-crystal structure of MNK2 in Complex With Inhibitor

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 Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AGLY70
AARG298
ACYS299
ACYS311
ACYS314

site_idAC2
Number of Residues11
Detailsbinding site for residue FZJ A 402
ChainResidue
AGLU160
ALYS161
AMET162
ACYS225
AASP226
AHOH502
AHOH503
AGLY91
AVAL98
AALA111
ALYS113

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAHARVQtCinlitsqe..........YAVK
ChainResidueDetails
ALEU90-LYS113

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKpeNILC
ChainResidueDetails
AILE201-CYS213

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
AASP205

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU90
ALYS113

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLU160

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16917500
ChainResidueDetails
AGLU209

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16216586, ECO:0000269|PubMed:16917500
ChainResidueDetails
ACYS299
ACYS311
ACYS314

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8CDB0
ChainResidueDetails
ASER74

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11463832
ChainResidueDetails
ATHR244
ATHR249
ATHR379

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PDB entries from 2024-07-17

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