Structure of PDB 4mp0 Chain A Binding Site BS02

Receptor Information
>4mp0 Chain A (length=295) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLEL
EAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETIC
LLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDC
FNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL
WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGY
EFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain4mp0 Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4mp0 Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code.
Resolution2.1003 Å
Binding residue
(original residue number in PDB)		D92 N124 H173 H248
Binding residue
(residue number reindexed from 1)		D87 N119 H168 H243
Annotation score1
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) D59 H61 D87 D90 R91 N119 H120 H168 R216 H243
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4mp0, PDBe:4mp0, PDBj:4mp0
PDBsum4mp0
PubMed24591642
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

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