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3ENM

The structure of the MAP2K MEK6 reveals an autoinhibitory dimer

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
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AASN89
ASER90
AGLN91
DARG121
DGLU122

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
AHOH402
APRO274
ASER275
ALYS297
AHOH358

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 4
ChainResidue
BVAL88
BASN89
BSER90
BGLN93
BLYS94
CARG121
CGLU122

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1
ChainResidue
BGLU68
BLYS82
BARG83
BLEU204
BVAL205
DGLY65

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 3
ChainResidue
BARG121
BGLU122
CASN89
CSER90
CGLN91
CHOH461

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 1
ChainResidue
AARG121
AGLU122
AGLY123
DASN89
DSER90
DGLN91

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAYGVVEkMrhvpsgqi..........MAVK
ChainResidueDetails
ALEU59-LYS82

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDVKpsNVLI
ChainResidueDetails
AVAL175-ILE187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP179
BASP179
CASP179
DASP179

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CLEU59
CLYS82
DLEU59
DLYS82
ALEU59
ALYS82
BLEU59
BLYS82

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by MAP3K; alternate => ECO:0000269|PubMed:16728640
ChainResidueDetails
AASP207
BASP207
CASP207
DASP207

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by MAP3K; alternate => ECO:0000269|PubMed:16728640
ChainResidueDetails
AASP211
BASP211
CASP211
DASP211

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PDB entries from 2024-06-12

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