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4U3Z

APO MAP4K4 T181E Phosphomimetic Mutant

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue MES A 401
ChainResidue
AMET275
BMET275
BGLN276
BHOH430
AGLN276
APRO278
AGLN282
AASP307
AARG308
AHOH519
AHOH537
AHOH538

site_idAC2
Number of Residues7
Detailsbinding site for residue MES A 402
ChainResidue
AHIS145
AILE146
ATYR212
ASER279
ATHR280
AGLU281
AHOH520

site_idAC3
Number of Residues7
Detailsbinding site for residue NA A 403
ChainResidue
ASER77
AHIS78
AHIS79
AILE82
ATHR84
AGLU106
AHOH701

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGNGTYGQVYkGrhvktgql..........AAIK
ChainResidueDetails
BVAL31-LYS54

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKgqNVLL
ChainResidueDetails
BVAL149-LEU161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
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 Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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