Structure of PDB 1e5s Chain B Binding Site BS01

Receptor Information
>1e5s Chain B (length=243) Species: 60871 (Streptomyces sp. TH1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRSHILGKIELDQTRLAPDLAYLAAVPTVEEFSNGFWKHVPLWNAPTAHV
EHVPYLKEIVTTVFDGTHLQMARSRNLKNAIVIPHRDFVYFRTFMVLEDS
PLAFHSNEDTVIHMRPGEIWFLDAATVHSAVNFSEISRQSLCVDFYAPGS
TPDLPERRPFTAEHRRRILSLGQVIERENFRDILFLLSKVHYKYDVHPSE
TYDWLIEISKQAGDEKMVVKAEQIRDFAVEARALSERFSLTSW
Ligand information
Ligand IDFE2
InChIInChI=1S/Fe/q+2
InChIKeyCWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Fe+2]
CACTVS 3.341[Fe++]
FormulaFe
NameFE (II) ION
ChEMBL
DrugBankDB14510
ZINC
PDB chain1e5s Chain B Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1e5s Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H107 D109 H158
Binding residue
(residue number reindexed from 1)		H85 D87 H128
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.11.28: proline 3-hydroxylase.
Gene Ontology
Molecular Function
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0033763 proline 3-hydroxylase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0018193 peptidyl-amino acid modification

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Molecular Function
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Biological Process
External links
PDB RCSB:1e5s, PDBe:1e5s, PDBj:1e5s
PDBsum1e5s
PubMed11737217
UniProtO09345|P3H2_STRSQ L-proline cis-3-hydroxylase 2

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