Structure of PDB 6y2n Chain A Binding Site BS02

Receptor Information
>6y2n Chain A (length=306) Species: 405948 (Saccharopolyspora erythraea NRRL 2338) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GRVDVAEKAMINSRADVNQLLPLKYGWAWEKYLAGCNNHWMPTEVSMQAD
IALWKSRDGLTDDERMMLKRNLGFFATAESLVANNIVLAVYRHITNPECR
QYLLRQAFEEAVHTHTFQYICESLGLDEGELFNMYREIPSISDKDAWALR
YTQNLENPIGTPEADQAFLRDLVAFYVIFEGMWFYTGFAQILSLGRRNKM
VGIAEQYQYILRDESIHLNFGIDCINQIKIENPHLWTPEFQEEVRTMLTE
ACELEVAYGRDTMPRGILGLNAGLCEEYMRFITNRRCAQLGLEPVFPETA
NPFPWM
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain6y2n Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6y2n Current status and future opportunities for serial crystallography at MAX IV Laboratory.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		E132 E205 E239 H242
Binding residue
(residue number reindexed from 1)		E110 E180 E214 H217
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6y2n, PDBe:6y2n, PDBj:6y2n
PDBsum6y2n
PubMed32876583
UniProtA4F980

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