Structure of PDB 3h69 Chain A

Receptor sequence
>3h69A (length=315) Species: 9606 (Homo sapiens) [Search protein sequence]
YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLST
LVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDR
GSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTA
QMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQP
PDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIR
SHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQ
FTAVPHPNVKPMAYA
3D structure
PDB3h69 Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) D67 H69 D96 D99 R100 N128 H129 H177 R225 H252
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A D271 N303 H352 H427 D96 N128 H177 H252
BS02 ZN A D242 H244 D271 D67 H69 D96
BS03 ENL A D242 H244 D271 R275 N303 H304 R400 H427 F446 Y451 D67 H69 D96 R100 N128 H129 R225 H252 F271 Y276
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:3h69, PDBe:3h69, PDBj:3h69
PDBsum3h69
PubMed19601647
UniProtP53041|PPP5_HUMAN Serine/threonine-protein phosphatase 5 (Gene Name=PPP5C)

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