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4ZK5

MAP4K4 in complex with inhibitor GNE-495

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 Residues4
Detailsbinding site for residue MG A 401
ChainResidue
ASER77
AHIS79
AILE82
ATHR84

site_idAC2
Number of Residues8
Detailsbinding site for residue MES A 402
ChainResidue
ALYS311
BMET275
BGLN276
AMET275
AGLN276
AARG277
APRO278
AGLN282

site_idAC3
Number of Residues14
Detailsbinding site for residue 4P4 A 403
ChainResidue
AVAL31
ATYR36
ALYS41
AALA52
ALYS54
AMET105
AGLU106
APHE107
ACYS108
AGLY109
AGLY111
ALEU160
AVAL170
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

239492

PDB entries from 2025-07-30

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