Structure of PDB 1nd6 Chain B Binding Site BS02

Receptor Information
>1nd6 Chain B (length=343) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELG
EYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIW
NPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLH
PYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTM
TKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKK
LIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYR
NETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTT
Ligand information
Ligand IDGLY
InChIInChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
InChIKeyDHMQDGOQFOQNFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C(=O)O)N
CACTVS 3.341NCC(O)=O
ACDLabs 10.04O=C(O)CN
FormulaC2 H5 N O2
NameGLYCINE
ChEMBLCHEMBL773
DrugBankDB00145
ZINCZINC000004658552
PDB chain1nd6 Chain B Residue 9000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1nd6 Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H1304 E1305 Y1307
Binding residue
(residue number reindexed from 1)		H305 E306 Y308
Annotation score1
Enzymatic activity
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:0005515 protein binding
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:0005634 nucleus
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005765 lysosomal membrane
GO:0005771 multivesicular body
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0012506 vesicle membrane
GO:0016020 membrane
GO:0030141 secretory granule
GO:0030175 filopodium
GO:0031985 Golgi cisterna
GO:0035577 azurophil granule membrane
GO:0045177 apical part of cell
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nd6, PDBe:1nd6, PDBj:1nd6
PDBsum1nd6
PubMed12525165
UniProtP15309|PPAP_HUMAN Prostatic acid phosphatase (Gene Name=ACP3)

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