Structure of PDB 8w7d Chain B

Receptor sequence
>8w7dB (length=467) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGL
VSDVFEARHMQRLQGNMGIGHVRYPTSSASEAQPFYVNSPYGITLAHNGN
LTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIF
AAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTE
YMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSNPCL
FEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPE
TSCDIALEIARILGKPYRQGFVKNRYVGRTFSVRRKLNANRAEFRDKNVL
LVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSAT
ELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNG
VYVTKDVDQGYLDFLDT
3D structure
PDB8w7d Uncommon Arrangement of Self-resistance Allows Biosynthesis of de novo Purine Biosynthesis Inhibitor that Acts as an Immunosuppressor
ChainB
Resolution2.81 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.2.14: amidophosphoribosyltransferase.
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 7TG B F255 Y259 F260 D368 S369 V371 R372 G373 T374 T375 M410 F251 Y255 F256 D354 S355 V357 R358 G359 T360 T361 M396
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004044 amidophosphoribosyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0097216 guanosine tetraphosphate 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
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8w7d, PDBe:8w7d, PDBj:8w7d
PDBsum8w7d
PubMed38051581
UniProtP0AG16|PUR1_ECOLI Amidophosphoribosyltransferase (Gene Name=purF)

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