Structure of PDB 1i2d Chain B

Receptor sequence
>1i2dB (length=572) Species: 5076 (Penicillium chrysogenum) [Search protein sequence]
ANAPHGGVLKDLLARDAPRQAELAAEAESLPAVTLTERQLCDLELIMNGG
FSPLEGFMNQADYDRVCEDNRLADGNVFSMPITLDASQEVIDEKKLQAGS
RITLRDFRDDRNLAILTIDDIYRPDKTKEAKLVFGGDPEHPAIVYLNNTV
KEFYIGGKIEAVNKLNHYDYVALRYTPAELRVHFDKLGWSRVVAFQTRNP
MHRAHRELTVRAARSRQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRY
PNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGSNS
KGEDFYGPYDAQHAVEKYKDELGIEVVEFQMVTYLPDTDEYRPVDQVPAG
VKTLNISGTELRRRLRSGAHIPEWFSYPEVVKILRESNPPRATQGFTIFL
TGYMNSGKDAIARALQVTLNQQGGRSVSLLLGDTVRHELSSELGFTREDR
HTNIQRIAFVATELTRAGAAVIAAPIAPYEESRKFARDAVSQAGSFFLVH
VATPLEHCEQSDKRGIYAAARRGEIKGFTGVDDPYETPEKADLVVDFSKQ
SVRSIVHEIILVLESQGFLERQ
3D structure
PDB1i2d Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation.
ChainB
Resolution2.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T198 R199 H203 H206 R292
Catalytic site (residue number reindexed from 1) T197 R198 H202 H205 R291
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 ADX B F196 Q197 T198 R199 L209 G291 R292 H294 A295 M332 F195 Q196 T197 R198 L208 G290 R291 H293 A294 M331
BS02 ADX B M405 D434 R437 F446 R451 N454 P476 I477 P479 G528 F529 T530 M404 D433 R436 F445 R450 N453 P475 I476 P478 G527 F528 T529
Gene Ontology
Molecular Function
GO:0004020 adenylylsulfate kinase activity
GO:0004781 sulfate adenylyltransferase (ATP) activity
GO:0005524 ATP binding
Biological Process
GO:0000103 sulfate assimilation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1i2d, PDBe:1i2d, PDBj:1i2d
PDBsum1i2d
PubMed11389593
UniProtQ12650|MET3_PENCH Sulfate adenylyltransferase (Gene Name=met3)

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