Structure of PDB 4nm5 Chain A

Receptor sequence
>4nm5A (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
GSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQA
KLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKK
DEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIH
SFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYR
APELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVL
GTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEY
TPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPL
ATILIPPHARH
3D structure
PDB4nm5 Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D181 K183 N186 D200 S219
Catalytic site (residue number reindexed from 1) D158 K160 N163 D177 S196
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
2.7.11.26: [tau protein] kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide A V263 D264 Y288 F291 F293 P294 I296 V240 D241 Y265 F268 F270 P271 I273
BS02 peptide A R92 F93 K94 R96 R180 K205 N213 V214 Y216 R69 F70 K71 R73 R157 K182 N190 V191 Y193
BS03 ADP A F67 A83 K85 D133 Y134 V135 L188 D200 F44 A60 K62 D110 Y111 V112 L165 D177
BS04 MG A N186 D200 N163 D177
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4nm5, PDBe:4nm5, PDBj:4nm5
PDBsum4nm5
PubMed24642411
UniProtP49841|GSK3B_HUMAN Glycogen synthase kinase-3 beta (Gene Name=GSK3B)

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