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8QRB

Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGAYGMVCsAydnlnkvrv.........AIKK
ChainResidueDetails
AILE29-LYS53

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpsNLLL
ChainResidueDetails
AVAL143-LEU155

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FehqtycqrtlREikillrfrheniigindiiraptieqmkdvyivqdlmetdlykllktqhlsndhicyflyqilrglkyihsanvlh..........RDlKpsnlllnttC
ChainResidueDetails
APHE57-CME159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP147

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:8639522
ChainResidueDetails
AILE29
ALYS52

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.2
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000250|UniProtKB:P28482
ChainResidueDetails
ASER27

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ATHR183

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ATYR185

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P28482
ChainResidueDetails
ATHR188

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28482
ChainResidueDetails
ASER244
ASER246
ASER282

234785

PDB entries from 2025-04-16

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