Structure of PDB 6alz Chain A

Receptor sequence
>6alzA (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELE
APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL
LLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCF
NCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW
SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYE
FFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
3D structure
PDB6alz PP1:Tautomycetin Complex Reveals a Path toward the Development of PP1-Specific Inhibitors.
ChainA
Resolution2.208 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D64 H66 D92 D95 R96 N124 H125 H173 R221 H248
Catalytic site (residue number reindexed from 1) D58 H60 D86 D89 R90 N118 H119 H167 R215 H242
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
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 MN A D92 N124 H173 H248 D86 N118 H167 H242
BS02 MN A D64 H66 D92 D58 H60 D86
BS03 BKM A R96 C127 S129 Y134 V195 W206 R221 V223 V250 Y272 F276 R90 C121 S123 Y128 V189 W200 R215 V217 V244 Y266 F270 PDBbind-CN: -logKd/Ki=10.42,IC50=38pM
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:6alz, PDBe:6alz, PDBj:6alz
PDBsum6alz
PubMed29156132
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

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