Structure of PDB 1bib Chain A

Receptor sequence
>1bibA (length=294) Species: 562 (Escherichia coli) [Search protein sequence]
KDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVF
TVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGEL
KSGDACIAEYQQAGRGRSPFGANLYLSMFWRLEQPAAAIGLSLVIGIVMA
EVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGAAQIVIGAGINMAMW
ITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFIN
RPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLR
3D structure
PDB1bib Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R118 K183 R317
Catalytic site (residue number reindexed from 1) R117 K175 R294
Enzyme Commision number 6.3.4.15: biotin--[biotin carboxyl-carrier protein] ligase.
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 BTN A S89 T90 N91 Q112 G115 R116 G186 G204 A205 S88 T89 N90 Q111 G114 R115 G178 G192 A193
Gene Ontology
Molecular Function
GO:0000976 transcription cis-regulatory region binding
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0004077 biotin--[biotin carboxyl-carrier protein] ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0009374 biotin binding
GO:0016874 ligase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006355 regulation of DNA-templated transcription
GO:0006768 biotin metabolic process
GO:0009102 biotin biosynthetic process
GO:0036211 protein modification process
Cellular Component
GO:0005737 cytoplasm
GO:0017053 transcription repressor complex

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Biological Process
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Cellular Component
External links
PDB RCSB:1bib, PDBe:1bib, PDBj:1bib
PDBsum1bib
PubMed1409631
UniProtP06709|BIRA_ECOLI Bifunctional ligase/repressor BirA (Gene Name=birA)

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