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3DV3

MEK1 with PF-04622664 Bound

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1
ChainResidue
AASN195
AASP208
AHOH9020
AHOH9078

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 9000
ChainResidue
ALYS97
AMET143
AGLU144
AMET146
ASER150
AGLN153
ALYS192
ASER194
AASN195
ALEU197
AASP208
AHOH9011
AHOH9020
AHOH9054
AHOH9069
AHOH9078
AHOH9079
AALA76
AGLY77
AASN78
AGLY80
AALA95

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MEK A 9001
ChainResidue
ALYS97
ALEU115
AILE141
AMET143
AASP208
APHE209
AGLY210
ASER212
ALEU215
AHOH9008
AHOH9011
AHOH9020

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 9003
ChainResidue
ALEU63
AGLN116
AHIS119
AGLY131
AALA132

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK
ChainResidueDetails
ALEU74-LYS97

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV
ChainResidueDetails
AILE186-VAL198

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 Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15543157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17880056","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18951019","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19019675","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19706763","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21310613","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19161339","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3EQF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by BRAF and RAF1","evidences":[{"source":"PubMed","id":"10409742","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20956560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29433126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8131746","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER194
AASP190

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS192
AASP190

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS192
ATHR226
AASP190

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS192
AASN195
AASP190

243911

PDB entries from 2025-10-29

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