Structure of PDB 1fjm Chain A Binding Site BS03

Receptor Information
>1fjm Chain A (length=294) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELE
APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICL
LLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCF
NCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLW
SDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYE
FFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
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 chain1fjm Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fjm Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D64 H66 D92
Binding residue
(residue number reindexed from 1)		D58 H60 D86
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) D58 H60 D86 D89 R90 N118 H119 H167 R215 H242
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0004721 phosphoprotein phosphatase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0017018 myosin phosphatase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0072542 protein phosphatase activator activity
GO:1901567 fatty acid derivative binding
Biological Process
GO:0005977 glycogen metabolic process
GO:0006446 regulation of translational initiation
GO:0006470 protein dephosphorylation
GO:0032922 circadian regulation of gene expression
GO:0042752 regulation of circadian rhythm
GO:0043153 entrainment of circadian clock by photoperiod
GO:0043558 regulation of translational initiation in response to stress
GO:0048511 rhythmic process
GO:0051301 cell division
GO:0090263 positive regulation of canonical Wnt signaling pathway
Cellular Component
GO:0000164 protein phosphatase type 1 complex
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0072357 PTW/PP1 phosphatase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fjm, PDBe:1fjm, PDBj:1fjm
PDBsum1fjm
PubMed7651533
UniProtP62139|PP1A_RABIT Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

[Back to BioLiP]