Structure of PDB 2pmk Chain A

Receptor sequence
>2pmkA (length=243) Species: 562 (Escherichia coli) [Search protein sequence]
HHDITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKL
IQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIIDNIS
LANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRI
AIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRL
STVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQLQSD
3D structure
PDB2pmk Water-mediated protein-fluorophore interactions modulate the affinity of an ABC-ATPase/TNP-ADP complex
ChainA
Resolution1.6 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 128 A Y477 G505 S506 G507 K508 S509 T510 K513 Y13 G41 S42 G43 K44 S45 T46 K49 PDBbind-CN: -logKd/Ki=5.92,Kd=1.2uM
BS02 ADP A Y477 I484 S504 G505 S506 G507 K508 S509 T510 Y13 I20 S40 G41 S42 G43 K44 S45 T46
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity

View graph for
Molecular Function
External links
PDB RCSB:2pmk, PDBe:2pmk, PDBj:2pmk
PDBsum2pmk
PubMed18155559
UniProtP08716|HLYBP_ECOLX Alpha-hemolysin translocation ATP-binding protein HlyB (Gene Name=hlyB)

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