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6YG1

Crystal structure of MKK7 (MAP2K7) in an active state, allosterically triggered by the N-terminal helix

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 501
ChainResidue
ASER189
AHIS190
ACYS192
AILE195
AGLN197
AHOH647

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 502
ChainResidue
AVAL161
AGLU213
ALEU214

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 503
ChainResidue
AILE115
AGLN118
ALEU187
ATHR201
AHOH707

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 504
ChainResidue
ATYR121
AARG128
AHOH674
BPHE345
CGLN353

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 505
ChainResidue
ATYR247
ALYS250
ALYS386
ATYR387
AASN388

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO A 506
ChainResidue
ALYS383
APRO385
ALYS386
ALYS389

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 507
ChainResidue
ATYR129
ATHR158
AGLU232
AARG398
ATYR399

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 508
ChainResidue
AGLN227
ATHR333
BASN340

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 509
ChainResidue
AILE280
AASP291
ASER293
AALA294

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO A 510
ChainResidue
ATYR299
AGLU330
AHOH677

site_idAD2
Number of Residues1
Detailsbinding site for residue EDO A 511
ChainResidue
ACYS341

site_idAD3
Number of Residues7
Detailsbinding site for residue EDO A 512
ChainResidue
AASP344
AASP344
APHE345
ALEU348
ALEU348
AHOH630
AHOH630

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO A 513
ChainResidue
APRO302
AASP306
ALYS379

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO A 514
ChainResidue
AASP306
APRO307

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO A 515
ChainResidue
APRO337
ATYR338
AASN340
ACYS341
BMET363

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO A 516
ChainResidue
AGLU354
AHOH656
BGLY364

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO A 517
ChainResidue
AASN176
AHOH624

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO A 518
ChainResidue
AASP306
ATHR349
AHOH622
AHOH634
AHOH700

site_idAE1
Number of Residues5
Detailsbinding site for residue NA B 501
ChainResidue
BSER189
BHIS190
BCYS192
BILE195
BGLN197

site_idAE2
Number of Residues4
Detailsbinding site for residue EDO B 502
ChainResidue
AGLY126
BTHR349
BLYS350
BGLU354

site_idAE3
Number of Residues3
Detailsbinding site for residue EDO B 503
ChainResidue
BTYR299
BGLU330
BHOH641

site_idAE4
Number of Residues3
Detailsbinding site for residue EDO B 504
ChainResidue
APRO310
ALYS342
BARG233

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO B 505
ChainResidue
BARG270
BVAL404
BASP405
BVAL406
BALA407

site_idAE6
Number of Residues6
Detailsbinding site for residue EDO B 506
ChainResidue
BALA297
BASP344
BLEU348
CASP344
CPHE345
CLEU348

site_idAE7
Number of Residues5
Detailsbinding site for residue NA C 501
ChainResidue
CCYS192
CILE195
CGLN197
CSER189
CHIS190

site_idAE8
Number of Residues7
Detailsbinding site for residue NA C 502
ChainResidue
CARG225
CMET414
CMET414
CALA415
CALA415
CTHR417
CTHR417

site_idAE9
Number of Residues3
Detailsbinding site for residue EDO C 503
ChainResidue
CLYS250
CTYR387
CASN388

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDVKpsNILL
ChainResidueDetails
AVAL255-LEU267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP259
BASP259
CASP259

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AMET142
ALYS165
BMET142
BLYS165
CMET142
CLYS165

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Cleavage; by anthrax lethal factor
ChainResidueDetails
AGLY92
BGLY92
CGLY92

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine; by MAP3K => ECO:0000250
ChainResidueDetails
AASP287
BASP287
CASP287

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine; by MAP3K => ECO:0000250
ChainResidueDetails
AASP291
BASP291
CASP291

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PDB entries from 2024-07-10

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