Structure of PDB 6dno Chain A

Receptor sequence

>6dnoA (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]

LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELE
APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL
LLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCF
NCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW
SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYE
FFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

3D structure

PDB

6dno Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme.

Chain

Resolution

1.45 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	peptide	A	R23 P24 R74 Y78 D242 Y255 F257 R261 L289 M290 C291 S292 F293 Q294 I295 L296 K297 P298 A299	R17 P18 R68 Y72 D236 Y249 F251 R255 L283 M284 C285 S286 F287 Q288 I289 L290 K291 P292 A293
BS02	peptide	A	R96 H125 Y134 D197 W206 D220 R221 Y272 C273 E275	R90 H119 Y128 D191 W200 D214 R215 Y266 C267 E269

Gene Ontology

	Molecular Function
GO:0016787	hydrolase activity

View graph for
Molecular Function

External links

PDB	RCSB:6dno, PDBe:6dno, PDBj:6dno
PDBsum	6dno
PubMed	30443599
UniProt	P62136\|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

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