Structure of PDB 4xww Chain B Binding Site BS04

Receptor Information
>4xww Chain B (length=543) Species: 1299 (Deinococcus radiodurans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APTLEVIPLGGMGEIGKNITVFRYGDEIVVVDGGLAFPKAHQMGIDLIVP
RIDYLLEHQDKIKGWILTHGHEDHIGGLPYIFARLPRVPVYGLPLTLALV
REKLSEFGLQDVDLREVTYGDEVRFGQSFVAEFFCMTHSIPDNAGYILKT
PVGDVLHTGDFKIDPDVGTGAGIVSDLERVEQAGKDGVLLLISDSTNAER
PGHTPSEAEIARNLEEIIKGCRGRVFLTTFASQVYRIQNILDLAHRQGRR
VVMEGRSMIKYAQAAQATGHMNPPEPFLTSEEVGELQDQQVLFVCTGSQG
QPMAVLGRLAFGTHAKIALRRGDTVILSSNPIPGNEDAVNLIVNRLYEIG
VDVVYPPTYRVHASGHASQEELATILNLTRPKFFLPWHGEPRHQINHAKL
AQTLPRPPKRTLIAKNGDIVNLGPDEFRVSGTVAAGAVYVDGLGVGDVND
DVLLDRVNLSQEGLLILTAVLHPTPHVEVVARGFARPNRDLELQIRRVAL
EAVEQGLREKKRLEDVRDDMYGAVRRFTRKATGRNPVLIPMIV
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 chain4xww Chain B Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4xww Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J
Resolution1.7 Å
Binding residue
(original residue number in PDB)
G59 D456
Binding residue
(residue number reindexed from 1)
G44 D441
Annotation score4
Enzymatic activity
Enzyme Commision number 3.1.-.-
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004519 endonuclease activity
GO:0004521 RNA endonuclease activity
GO:0004527 exonuclease activity
GO:0004534 5'-3' RNA exonuclease activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006364 rRNA processing
GO:0006396 RNA processing
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:4xww, PDBe:4xww, PDBj:4xww
PDBsum4xww
PubMed25940620
UniProtH9CZL7

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