Structure of PDB 1ecb Chain C

Receptor sequence
>1ecbC (length=482) Species: 562 (Escherichia coli) [Search protein sequence]
CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGL
VSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAH
NGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEAD
NIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDEN
RTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSN
PCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIP
IPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKL
NANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIR
FPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAEN
PDIQQFECSVFNGVYVTKDVDQGYLDFLDTLR
3D structure
PDB1ecb Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG C D366 D367 D366 D367
BS02 5GP C Y74 Y258 D366 D367 V370 R371 G372 T374 Y74 Y258 D366 D367 V370 R371 G372 T374
BS03 5GP C H25 Y258 R261 P302 E303 T304 K326 H25 Y258 R261 P302 E303 T304 K326
BS04 5GP C V325 K326 R328 V325 K326 R328
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1ecb, PDBe:1ecb, PDBj:1ecb
PDBsum1ecb
PubMed9333323
UniProtP0AG16|PUR1_ECOLI Amidophosphoribosyltransferase (Gene Name=purF)

[Back to BioLiP]