Structure of PDB 1qp0 Chain A

Receptor sequence
>1qp0A (length=338) Species: 562 (Escherichia coli) [Search protein sequence]
TIKDVAKRANVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVAR
SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLE
KQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKA
DFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMK
AMEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAM
GALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAF
NMLLDRIVNKREEPQSIEVHPRLIERRSVADGPFRDYR
3D structure
PDB1qp0 The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions.
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna A S14 T16 T17 R26 V28 A29 T32 L54 K55 S12 T14 T15 R24 V26 A27 T30 L52 K53 PDBbind-CN: Kd=35nM
BS02 HPA A Y73 F74 R190 T192 R196 F221 D275 Y71 F72 R188 T190 R194 F219 D273
Gene Ontology
Molecular Function
GO:0000976 transcription cis-regulatory region binding
GO:0001217 DNA-binding transcription repressor activity
GO:0002057 guanine binding
GO:0003677 DNA binding
GO:0003700 DNA-binding transcription factor activity
GO:0005515 protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006355 regulation of DNA-templated transcription
GO:0045892 negative regulation of DNA-templated transcription
GO:1900372 negative regulation of purine nucleotide biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1qp0, PDBe:1qp0, PDBj:1qp0
PDBsum1qp0
PubMed10438625
UniProtP0ACP7|PURR_ECOLI HTH-type transcriptional repressor PurR (Gene Name=purR)

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