Structure of PDB 2fgk Chain A

Receptor sequence
>2fgkA (length=241) Species: 562 (Escherichia coli) [Search protein sequence]
DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQ
RFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIIDNISLA
NPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAI
ARALVNNPKILIFDQATSALDYESEHVIMRNMHKICKGRTVIIIAHRLST
VKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQLQSD
3D structure
PDB2fgk A structural analysis of asymmetry required for catalytic activity of an ABC-ATPase domain dimer.
ChainA
Resolution2.7 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 ATP A Y477 I484 S504 G505 S506 G507 K508 S509 T510 H662 Y11 I18 S38 G39 S40 G41 K42 S43 T44 H196
BS02 ATP A G605 S607 G609 Q610 G139 S141 G143 Q144
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity

View graph for
Molecular Function
External links
PDB RCSB:2fgk, PDBe:2fgk, PDBj:2fgk
PDBsum2fgk
PubMed16858415
UniProtP08716|HLYBP_ECOLX Alpha-hemolysin translocation ATP-binding protein HlyB (Gene Name=hlyB)

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