Structure of PDB 1ao0 Chain A

Receptor sequence
>1ao0A (length=455) Species: 1423 (Bacillus subtilis) [Search protein sequence]
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLI
TEVFQNGELSKVKGKGAIGHVRYATGYENVQPLLFRSQNNGSLALAHNGN
LVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNSLSML
KGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDVVGAT
YLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNIDGIN
VHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYELGLI
KNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVRGTTS
RRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHSVEEI
RQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIYQDTV
LPHVK
3D structure
PDB1ao0 Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C1 G27 N102 G103 Y242 E300 K305 Q315 K423
Catalytic site (residue number reindexed from 1) C1 G27 N98 G99 Y238 E296 K301 Q311 K419
Enzyme Commision number 2.4.2.14: amidophosphoribosyltransferase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004044 amidophosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0006541 glutamine metabolic process
GO:0009113 purine nucleobase biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1ao0, PDBe:1ao0, PDBj:1ao0
PDBsum1ao0
PubMed9271502
UniProtP00497|PUR1_BACSU Amidophosphoribosyltransferase (Gene Name=purF)

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