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4UYA

Structure of MLK4 kinase domain with ATPgammaS

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 Residues14
DetailsBINDING SITE FOR RESIDUE AGS A 1438
ChainResidue
AVAL138
ALEU270
AASP289
AMG1439
AMG1440
AHOH2038
AALA149
AILE184
ALEU200
AGLU201
AALA203
AASP263
ALYS265
AASN268

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1439
ChainResidue
ALYS265
AASN268
AAGS1438
AMG1440

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1440
ChainResidue
ALYS265
AAGS1438
AMG1439
AHOH2039

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGGFGQVYrAtwqgqe............VAVK
ChainResidueDetails
AILE130-LYS151

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKssNILL
ChainResidueDetails
AILE259-LEU271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q02779","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q02779","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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