Structure of PDB 4nm7 Chain A

Receptor sequence
>4nm7A (length=355) Species: 9606 (Homo sapiens) [Search protein sequence]
SMKVSRDSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCD
SGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSKKDEVYLN
LVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICH
RDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIF
GATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE
QIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARL
TPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIP
PHARH
3D structure
PDB4nm7 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) D152 K154 N157 D171 S190
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 V234 D235 Y259 F262 F264 P265 I267
BS02 peptide A R92 F93 K94 R96 R180 K205 N213 V214 I217 R65 F66 K67 R69 R151 K176 N184 V185 I188
BS03 ADP A F67 A83 K85 D133 Y134 V135 L188 D200 F40 A56 K58 D104 Y105 V106 L159 D171
BS04 MG A N186 D200 N157 D171
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4nm7, PDBe:4nm7, PDBj:4nm7
PDBsum4nm7
PubMed24642411
UniProtP49841|GSK3B_HUMAN Glycogen synthase kinase-3 beta (Gene Name=GSK3B)

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