Structure of PDB 2gks Chain B

Receptor sequence
>2gksB (length=529) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
KIKYLKSIQISQRSVLDLELLAVGAFTPLDRFMGEEDYRNVVESMRLKSG
TLFPIPITLPMEKEIAKDLKEGEWIVLRDPKNVPLAIMRVEEVYKWNLEY
EAKNVLGTTDPRHPLVAEMHTWGEYYISGELKVIQLPKYYDFPEYRKTPK
QVREEIKSLGLDKIVAFQTRNPMHRVHEELTKRAMEKVGGGLLLHPVVGL
TKPGDVDVYTRMRIYKVLYEKYYDKKKTILAFLPLAMRMAGPREALWHGI
IRRNYGATHFIVGRDHASPGKDSKGKPFYDPYEAQELFKKYEDEIGIKMV
PFEELVYVPELDQYVEINEIRENFLKQGRKLPEWFTRPEVAEILAETYVP
KHKQGFCVWLTGLPCAGKSTIAEILATMLQARGRKVTLLDGDVVRTHLSR
GLGFSKEDRITNILRVGFVASEIVKHNGVVICALVSPYRSARNQVRNMME
EGKFIEVFVDAPVEVCEERDVKGLYKKAKEGLIKGFTGVDDPYEPPVAPE
VRVDTTKLTPEESALKILEFLKKEGFIKD
3D structure
PDB2gks Crystal structure of the bifunctional ATP sulfurylase-APS kinase from the chemolithotrophic thermophile Aquifex aeolicus.
ChainB
Resolution2.31 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T171 R172 H176 H179 R266
Catalytic site (residue number reindexed from 1) T169 R170 H174 H177 R264
Enzyme Commision number 2.7.1.25: adenylyl-sulfate kinase.
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 ADP B F169 Q170 T171 R172 N173 H179 L182 G265 R266 H268 A269 E306 L307 F167 Q168 T169 R170 N171 H177 L180 G263 R264 H266 A267 E304 L305
BS02 ADP B C382 G384 K385 S386 T387 R486 K496 C365 G367 K368 S369 T370 R469 K479
Gene Ontology
Molecular Function
GO:0004020 adenylylsulfate kinase activity
GO:0004781 sulfate adenylyltransferase (ATP) activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016779 nucleotidyltransferase activity
Biological Process
GO:0000103 sulfate assimilation
GO:0006790 sulfur compound metabolic process
GO:0010134 sulfate assimilation via adenylyl sulfate reduction
GO:0016310 phosphorylation
GO:0019379 sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)
GO:0070814 hydrogen sulfide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2gks, PDBe:2gks, PDBj:2gks
PDBsum2gks
PubMed17095009
UniProtO67174|SATC_AQUAE Probable bifunctional SAT/APS kinase (Gene Name=sat/cysC)

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