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4U45

MAP4K4 in complex with inhibitor (compound 25)

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 Residues5
Detailsbinding site for residue MG A 401
ChainResidue
ASER77
AHIS79
AILE82
ATHR84
AHOH552

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 402
ChainResidue
AHIS78
AHIS143
AHIS147

site_idAC3
Number of Residues12
Detailsbinding site for residue 3DC A 403
ChainResidue
AVAL39
AALA52
ALYS54
AMET105
AGLU106
APHE107
ACYS108
AGLY111
ALEU160
AVAL170
AASP171
AVAL31

site_idAC4
Number of Residues8
Detailsbinding site for residue MES B 401
ChainResidue
AARG213
AMET275
AGLN276
AARG277
AGLN282
AARG310
BMET275
BGLN276

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGNGTYGQVYkGrhvktgql..........AAIK
ChainResidueDetails
AVAL31-LYS54

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKgqNVLL
ChainResidueDetails
AVAL149-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 Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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