Structure of PDB 2obm Chain A

Receptor sequence
>2obmA (length=340) Species: 574521 (Escherichia coli O127:H6 str. E2348/69) [Search protein sequence]
HKIRVGDALLGRLIDGIGRPMESNIVAPYLPFERSLYAEPPRQVIDQPFI
LGVRAIDGLLTCGIGQRIGIFAGSGVGKSTLLGMICNGASADIIVLALIG
ERGREVNEFLALLPQSTLSKCVLVVTTSDRPALERMKAAFTATTIAEYFR
DQGKNVLLMMDSVTRYARAARDVGLASGEPDVRGGFPPSVFSSLPKLLER
AGPAPKGSITAIYTVLLESDNVNDPIGDEVRSILDGHIVLTRELAEENHF
PAIDIGLSASRVMHNVVTSEHLRAAAECKKLIATYKNPELLIRIGEYMGQ
DPEADKAIKNRKLIQNFIQQSTKDISSYEKTIESLFKVVA
3D structure
PDB2obm Structural analysis of a prototypical ATPase from the type III secretion system.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K183 E206 R207 R366
Catalytic site (residue number reindexed from 1) K78 E101 R102 R261
Enzyme Commision number 7.4.2.8: protein-secreting ATPase.
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 CA A N328 D333 N223 D228
BS02 ADP A G180 G182 K183 S184 T185 F355 T428 G75 G77 K78 S79 T80 F250 T322
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0009058 biosynthetic process
GO:0030254 protein secretion by the type III secretion system
Cellular Component
GO:0005737 cytoplasm
GO:0030257 type III protein secretion system complex

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Cellular Component
External links
PDB RCSB:2obm, PDBe:2obm, PDBj:2obm
PDBsum2obm
PubMed17237797
UniProtB7UMA6

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