Structure of PDB 1s95 Chain B Binding Site BS02
Receptor Information
>1s95 Chain B (length=325) Species:
9606
(Homo sapiens) [
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EYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLS
TLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVD
RGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYT
AQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQ
PPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYII
RSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFH
QFTAVPHPNVKPMAYANTLLQLGMM
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
1s95 Chain B Residue 602 [
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Receptor-Ligand Complex Structure
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PDB
1s95
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
D271 N303 H352 H427
Binding residue
(residue number reindexed from 1)
D97 N129 H178 H253
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D242 H244 D271 D274 R275 N303 H304 H352 R400 H427
Catalytic site (residue number reindexed from 1)
D68 H70 D97 D100 R101 N129 H130 H178 R226 H253
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:1s95
,
PDBe:1s95
,
PDBj:1s95
PDBsum
1s95
PubMed
15155720
UniProt
P53041
|PPP5_HUMAN Serine/threonine-protein phosphatase 5 (Gene Name=PPP5C)
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