Structure of PDB 1ecg Chain B

Receptor sequence
>1ecgB (length=500) Species: 562 (Escherichia coli) [Search protein sequence]
CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGL
VSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAH
NGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEAD
NIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDEN
RTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSN
PCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIP
IPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKL
NANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIR
FPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAEN
PDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQNEVENLEM
3D structure
PDB1ecg Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site.
ChainB
Resolution2.3 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 N101 G102 Y258 R321 K326 M336 D444
Catalytic site (residue number reindexed from 1) C1 G27 N101 G102 Y258 R321 K326 M336 D444
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 ONL B C1 T76 S79 N101 G102 S126 D127 C1 T76 S79 N101 G102 S126 D127
BS02 PIN B Y258 T304 D367 S368 I369 V370 G372 T373 T374 S375 Y258 T304 D367 S368 I369 V370 G372 T373 T374 S375
BS03 PIN B R45 K46 R62 E84 R45 K46 R62 E84
BS04 PIN B Y89 V90 N91 Y89 V90 N91
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:1ecg, PDBe:1ecg, PDBj:1ecg
PDBsum1ecg
PubMed8663035
UniProtP0AG16|PUR1_ECOLI Amidophosphoribosyltransferase (Gene Name=purF)

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