Structure of PDB 6omp Chain B Binding Site BS01

Receptor Information
>6omp Chain B (length=356) Species: 58346 (Streptomyces platensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MEKLWLNSADSHVLEPDDLWERALPAALRDRAPRCVRDNGRETVYVDGQV
VRRDPLDFADAMRPPGALDHHIRLKDLDDQGIWGEVVFPSRGLWTAVMTD
PVLARECIKVYNDWLKSDFLSLSPRLVGAAMVSMLDTDDAVAELRRAADL
GYQTVFLAATPPPGREFNMDVWEPLWAAAEEAGMTVSIHIGTGADTVVAR
GPGGAVINYVETLFPAQRAVAQLVASGALDRHPGLRVLIAEAGCAWVPAL
ADRMDEAYRQHGMFVRPKLSMLPGELVRRQVYASFQHDETAIGAVTAMNY
TNVLWGSDYPHLEGTFPRTQEVVTELFAGVDPEVRDLITRRNFTDLFTVP
ALPATV
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6omp Chain B Residue 406 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6omp Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.
Resolution1.7 Å
Binding residue
(original residue number in PDB)
D10 H12 H189 E241 D308
Binding residue
(residue number reindexed from 1)
D10 H12 H189 E241 D308
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016829 lyase activity
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0019748 secondary metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6omp, PDBe:6omp, PDBj:6omp
PDBsum6omp
PubMed31291107
UniProtA0A0A0UVH9

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