Structure of PDB 1ute Chain A Binding Site BS01

Receptor Information
>1ute Chain A (length=302) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTPILRFVAVGDWGGVPNAPFHTAREMANAKAIATTVKTLGADFILSLGD
NFYFTGVHDAKDKRFQETFEDVFSDPSLRNVPWHVLAGNHDHLGNVSAQI
AYSKISKRWNFPSPYYRLRFKIPRSNVSVAIFMLDTVTLCGNSDDFVSQQ
PERPRNLALARTQLAWIKKQLAAAKEDYVLVAGHYPVWSIAEHGPTHCLV
KQLLPLLTTHKVTAYLCGHDHNLQYLQDENGLGFVLSGAGNFMDPSKKHL
RKVPNGYLRFHFGAENSLGGFAYVEITPKEMSVTYIEASGKSLFKTKLPR
RA
Ligand information
Ligand IDFEO
InChIInChI=1S/2Fe.O
InChIKeyNPMYUMBHPJGBFA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Fe]O[Fe]
OpenEye OEToolkits 1.5.0O([Fe])[Fe]
FormulaFe2 O
NameMU-OXO-DIIRON
ChEMBL
DrugBank
ZINC
PDB chain1ute Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ute Crystal structure of mammalian purple acid phosphatase.
Resolution1.55 Å
Binding residue
(original residue number in PDB)		D14 D52 Y55 N91 H186 H221 H223
Binding residue
(residue number reindexed from 1)		D12 D50 Y53 N89 H184 H219 H221
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.2: acid phosphatase.
Gene Ontology
Molecular Function
GO:0003993 acid phosphatase activity
GO:0008198 ferrous iron binding
GO:0008199 ferric iron binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0006826 iron ion transport
GO:0045453 bone resorption
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ute, PDBe:1ute, PDBj:1ute
PDBsum1ute
PubMed10425678
UniProtP09889|PPA5_PIG Tartrate-resistant acid phosphatase type 5 (Gene Name=ACP5)

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