Structure of PDB 1rpt Chain A Binding Site BS01

Receptor Information
>1rpt Chain A (length=342) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KELKFVTLVFRHGDRGPIETFPNDPIKESSWPQGFGQLTKWGMGQHYELG
SYIRRRYGRFLNNSYKHDQVYIRSTDVDRTLMSAMTNLAALFPPEGNSIW
NPRLLWQPIPVHTVSLSEDRLLYLPFRDCPRFQELKSETLKSEEFLKRLQ
PYKSFIDTLPSLSGFEDQDLFEIWSRLYDPLYCESVHNFTLPTWATEDAM
TKLKELSELSLLSLYGIHKQKEKSRLQGGVLVNEILKNMKLATQPQKARK
LIMYSAHDTTVSGLQMALDVYNGLLPPYASCHIMELYQDNGGHFVEMYYR
NETQNEPYPLTLPGCTHSCPLEKFAELLDPVIPQDWATECMG
Ligand information
Ligand IDVO4
InChIInChI=1S/4O.V/q;3*-1;
InChIKeyLSGOVYNHVSXFFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		[O-][V]([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-][V](=O)([O-])[O-]
FormulaO4 V
NameVANADATE ION
ChEMBL
DrugBank
ZINC
PDB chain1rpt Chain A Residue 343 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1rpt Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		R11 H12 R15 R79 H257 D258
Binding residue
(residue number reindexed from 1)		R11 H12 R15 R79 H257 D258
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R11 H12 R15 R79 H257 D258
Catalytic site (residue number reindexed from 1) R11 H12 R15 R79 H257 D258
Enzyme Commision number 3.1.3.2: acid phosphatase.
3.1.3.48: protein-tyrosine-phosphatase.
3.1.3.5: 5'-nucleotidase.
Gene Ontology
Molecular Function
GO:0003993 acid phosphatase activity
GO:0004725 protein tyrosine phosphatase activity
GO:0008253 5'-nucleotidase activity
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0033265 choline binding
GO:0042131 thiamine phosphate phosphatase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0052642 lysophosphatidic acid phosphatase activity
GO:0060090 molecular adaptor activity
GO:0106411 XMP 5'-nucleosidase activity
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0006629 lipid metabolic process
GO:0006772 thiamine metabolic process
GO:0007040 lysosome organization
GO:0009117 nucleotide metabolic process
GO:0016311 dephosphorylation
GO:0046085 adenosine metabolic process
GO:0051930 regulation of sensory perception of pain
GO:0060168 positive regulation of adenosine receptor signaling pathway
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005764 lysosome
GO:0005765 lysosomal membrane
GO:0005771 multivesicular body
GO:0005886 plasma membrane
GO:0012506 vesicle membrane
GO:0016020 membrane
GO:0030141 secretory granule
GO:0030175 filopodium
GO:0031985 Golgi cisterna
GO:0045177 apical part of cell

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rpt, PDBe:1rpt, PDBj:1rpt
PDBsum1rpt
PubMed8168503
UniProtP20646|PPAP_RAT Prostatic acid phosphatase (Gene Name=Acp3)

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