Structure of PDB 1s95 Chain B Binding Site BS02

Receptor Information
>1s95 Chain B (length=325) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLS
TLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVD
RGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYT
AQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQ
PPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYII
RSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFH
QFTAVPHPNVKPMAYANTLLQLGMM
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 chain1s95 Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1s95 Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.
Resolution1.6 Å
Binding residue
(original residue number in PDB)
D271 N303 H352 H427
Binding residue
(residue number reindexed from 1)
D97 N129 H178 H253
Annotation score1
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
PDBsum1s95
PubMed15155720
UniProtP53041|PPP5_HUMAN Serine/threonine-protein phosphatase 5 (Gene Name=PPP5C)

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