Structure of PDB 6gp2 Chain A Binding Site BS01

Receptor Information
>6gp2 Chain A (length=318) Species: 265311 (Mesoplasma florum L1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GHMASIKNQYYNESVSPIEYAQQGFKGKMRSVNWNVVNDEKDLEVWNRIT
QNFWLPEKIPVSNDLTSWRTLTPEWQELITRTFTGLTLLDTIQATVGDVA
QVPNSLTDHEQVIYTNFAFMVAVHARSYGSIFSTLCSSEQIEEAHEWVIN
TETLQERAKALIPYYVNDDPLKSKVAAALMPGFLLYGGFYLPFYLSARGK
LPNTSDIIRLILRDKVIHNYYSGYKYQKKVAKLSPEKQAEMKEFVFKLLY
ELIDLEKAYLKELYEDFGLADDAIRFSVYNAGKFLQNLGYDSPFTEEETR
IEPEIFTQLSARADDWEF
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain6gp2 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6gp2 Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens.
Resolution1.48 Å
Binding residue
(original residue number in PDB)
G266 D269 D270
Binding residue
(residue number reindexed from 1)
G268 D271 D272
Annotation score1
Enzymatic activity
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
Cellular Component
GO:0005971 ribonucleoside-diphosphate reductase complex
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6gp2, PDBe:6gp2, PDBj:6gp2
PDBsum6gp2
PubMed30429545
UniProtQ6F0T5

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