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7NTH

Structure of TAK1 in complex with compound 54

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 GOL A 1001
ChainResidue
APRO121
AGLN299
ATYR300
APRO301
AHIS495

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 1002
ChainResidue
AHOH1158
AHOH1189
AHOH1224
AARG289
ATYR290
AGLN303
AASP494

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 1003
ChainResidue
ASER132
ATHR169
AASP295

site_idAC4
Number of Residues4
Detailsbinding site for residue DMS A 1004
ChainResidue
APRO258
ATYR488
ATRP491
AHOH1278

site_idAC5
Number of Residues24
Detailsbinding site for residue URW A 1005
ChainResidue
AVAL42
AGLY43
AARG44
AGLY45
ALYS63
AVAL90
AMET104
AGLU105
ATYR106
AALA107
AGLY109
AGLY110
ASER111
AASN114
APRO160
ALEU162
ALEU163
AASP175
AHOH1114
AHOH1131
AHOH1219
AHOH1255
AHOH1267
AHOH1276

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGAFGVVCkAkwrakd............VAIK
ChainResidueDetails
AVAL42-LYS63

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDLKppNLLL
ChainResidueDetails
ALEU152-LEU164

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 Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"10702308","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10838074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22406003","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q62073","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Required for interaction with MAP3K7","evidences":[{"source":"PubMed","id":"11323434","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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