Structure of PDB 1gph Chain 3

Receptor sequence
>1gph3 (length=465) Species: 1423 (Bacillus subtilis) [Search protein sequence]
CGVFGIWGHEEAPQITYYGLHSLQHRGQEGAGIVATDGEKLTAHKGQGLI
TEVFQNGELSKVKGKGAIGHVRYATAGGGGYENVQPLLFRSQNNGSLALA
HNGNLVNATQLKQQLENQGSIFQTSSDTEVLAHLIKRSGHFTLKDQIKNS
LSMLKGAYAFLIMTETEMIVALDPNGLRPLSIGMMGDAYVVASETCAFDV
VGATYLREVEPGEMLIINDEGMKSERFSMNINRSICSMEYIYFSRPDSNI
DGINVHSARKNLGKMLAQESAVEADVVTGVPDSSISAAIGYAEATGIPYE
LGLIKNRYVGRTFIQPSQALREQGVRMKLSAVRGVVEGKRVVMVDDSIVR
GTTSRRIVTMLREAGATEVHVKISSPPIAHPCFYGIDTSTHEELIASSHS
VDEIRQEIGADTLSFLSVEGLLKGIGRKYDDSNCGQCLACFTGKYPTEIY
QDTVLPHVKEAVLTK
3D structure
PDB1gph Structure of the allosteric regulatory enzyme of purine biosynthesis.
Chain3
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E300 K305 Q315 K423
Catalytic site (residue number reindexed from 1) E300 K305 Q315 K423
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
View graph for
Biological Process
External links
PDB RCSB:1gph, PDBe:1gph, PDBj:1gph
PDBsum1gph
PubMed8197456
UniProtP00497|PUR1_BACSU Amidophosphoribosyltransferase (Gene Name=purF)

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