Structure of PDB 1jhd Chain A

Receptor sequence
>1jhdA (length=396) Species: 35843 (sulfur-oxidizing endosymbiont of Riftia pachyptila) [Search protein sequence]
MIKPVGSDELKPLFVYDPEEHHKLSHEAESLPSVVISSQAAGNAVMMGAG
YFSPLQGFMNVADAMGAAEKMTLSDGSFFPVPVLCLLENTDAIGDAKRIA
LRDPNVEGNPVLAVMDIEAIEEVSDEQMAVMTDKVYRTTDMDHIGVKTFN
SQGRVAVSGPIQVLNFSYFQADFPDTFRTAVEIRNEIKEHGWSKVVAFQT
RNPMHRAHEELCRMAMESLDADGVVVHMLLGKLKKGDIPAPVRDAAIRTM
AEVYFPPNTVMVTGYGFDMLYAGPREAVLHAYFRQNMGATHFIIGRDHAG
VGDYYGAFDAQTIFDDEVPEGAMEIEIFRADHTAYSKKLNKIVMMRDVPD
HTKEDFVLLSGTKVREMLGQGIAPPPEFSRPEVAKILMDYYQSINS
3D structure
PDB1jhd Crystal structure of ATP sulfurylase from the bacterial symbiont of the hydrothermal vent tubeworm Riftia pachyptila.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T200 R201 H205 H208 R296
Catalytic site (residue number reindexed from 1) T200 R201 H205 H208 R296
Enzyme Commision number 2.7.7.4: sulfate adenylyltransferase.
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 SO4 A S7 D8 K11 S7 D8 K11
BS02 SO4 A N202 H208 R365 N202 H208 R365
BS03 SO4 A A207 H208 H332 T333 A207 H208 H332 T333
Gene Ontology
Molecular Function
GO:0004781 sulfate adenylyltransferase (ATP) activity
Biological Process
GO:0000103 sulfate assimilation

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Molecular Function
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Biological Process
External links
PDB RCSB:1jhd, PDBe:1jhd, PDBj:1jhd
PDBsum1jhd
PubMed11724564
UniProtQ54506|SAT_RIFPS Sulfate adenylyltransferase (Gene Name=sat)

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