Structure of PDB 3e7a Chain B

Receptor sequence
>3e7aB (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELE
APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL
LLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCF
NCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW
SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYE
FFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
3D structure
PDB3e7a Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
ChainB
Resolution1.63 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 B R96 S129 Y134 P196 D197 W206 R221 V223 Y272 C273 F276 R90 S123 Y128 P190 D191 W200 R215 V217 Y266 C267 F270
BS02 MN B D64 H66 D92 D58 H60 D86
BS03 MN B D92 N124 H173 H248 D86 N118 H167 H242
BS04 AZI B A128 S129 R132 A122 S123 R126
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:3e7a, PDBe:3e7a, PDBj:3e7a
PDBsum3e7a
PubMed18992256
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

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