Structure of PDB 1fqo Chain B

Receptor sequence

>1fqoB (length=266) Species: 562 (Escherichia coli)

MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYK
ALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIP
AENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPA
SSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVM
ILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVK
TLRYFNELEAENIKGL

3D structure

• PDB: 1fqo Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D72 D141 H143 E148
• Catalytic site (residue number reindexed from 1): D72 D141 H143 E148
• Enzyme Commision number: 3.5.99.6: glucosamine-6-phosphate deaminase.

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	F6R	B	S151 S152 R158 I159 K160	S151 S152 R158 I159 K160
BS02	F6R	B	P40 T41 G42 G43 T44 D72 G137 H143 A145	P40 T41 G42 G43 T44 D72 G137 H143 A145

Gene Ontology

Molecular Function

• GO:0004342 glucosamine-6-phosphate deaminase activity
• GO:0005515 protein binding
• GO:0016787 hydrolase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006043 glucosamine catabolic process
• GO:0006044 N-acetylglucosamine metabolic process
• GO:0006046 N-acetylglucosamine catabolic process
• GO:0006048 UDP-N-acetylglucosamine biosynthetic process
• GO:0019262 N-acetylneuraminate catabolic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1fqo, PDBe:1fqo, PDBj:1fqo
• PDBsum: 1fqo
• PubMed: 11752775
• UniProt: P0A759|NAGB_ECOLI Glucosamine-6-phosphate deaminase (Gene Name=nagB)