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4RVT

MAP4K4 in complex with a pyridin-2(1H)-one derivative

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 Residues8
DetailsBINDING SITE FOR RESIDUE 3XM A 401
ChainResidue
ATYR36
AVAL39
AALA52
AGLU106
APHE107
ACYS108
AGLY109
ALEU160

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES A 402
ChainResidue
AGLN276
AGLN282
BMET275
BGLN276
AMET275

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP153
BASP153

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL31
ALYS54
BVAL31
BLYS54

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER5
BSER5

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P97820
ChainResidueDetails
ASER324
BSER324

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PDB entries from 2024-07-24

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