Structure of PDB 1fjm Chain A Binding Site BS02
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 ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1fjm Chain A Residue 400 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
1fjm
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
D92 N124 H173 H248
Binding residue
(residue number reindexed from 1)
D86 N118 H167 H242
Annotation score
1
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
PDBsum
1fjm
PubMed
7651533
UniProt
P62139
|PP1A_RABIT Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)
[
Back to BioLiP
]