Structure of PDB 1ecc Chain B

Receptor sequence

>1eccB (length=492) Species: 562 (Escherichia coli) [Search protein sequence]

CGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGL
VSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAH
NGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEAD
NIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDEN
RTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSN
PCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIP
IPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKL
NANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIR
FPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAEN
PDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQ

3D structure

PDB

1ecc Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site.

Chain

Resolution

2.4 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)
BS01	MN	B	E376 I428	E376 I428
BS02	ONL	B	C1 R73 Y74 T76 A77 Q86 N101 G102 D127 S128	C1 R73 Y74 T76 A77 Q86 N101 G102 D127 S128
BS03	PCP	B	Y258 E303 T304 R332 T333 F334 K349 D366 D367 S368 V370 R371 G372 T373 T374	Y258 E303 T304 R332 T333 F334 K349 D366 D367 S368 V370 R371 G372 T373 T374

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

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1ecc, PDBe:1ecc, PDBj:1ecc
PDBsum	1ecc
PubMed	9333323
UniProt	P0AG16\|PUR1_ECOLI Amidophosphoribosyltransferase (Gene Name=purF)

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