Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4U44

MAP4K4 in complex with inhibitor (compound 16)

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 Residues6
Detailsbinding site for residue MES A 401
ChainResidue
AMET275
AGLN276
AGLN282
AHOH511
BMET275
BGLN276

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 402
ChainResidue
ATHR84
ASER77
AHIS79
AILE82

site_idAC3
Number of Residues11
Detailsbinding site for residue 3D9 A 403
ChainResidue
AVAL31
AASN33
AVAL39
AALA52
ALYS54
AGLU106
ACYS108
AGLY109
AGLY111
ALEU160
AASP171

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

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon