Structure of PDB 1dea Chain A

Receptor sequence
>1deaA (length=266) Species: 562 (Escherichia coli) [Search protein sequence]
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYK
ALVEMHKAGQVSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIP
AENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPA
SSLASRTRIKTLTHDTRVANSRFFDNDVNQVPKYALTVGVGTLLDAEEVM
ILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCDEPSTMELKVK
TLRYFNELEAENIKGL
3D structure
PDB1dea Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 PO4 A G42 G43 T44 R172 G42 G43 T44 R172
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1dea, PDBe:1dea, PDBj:1dea
PDBsum1dea
PubMed8747459
UniProtP0A759|NAGB_ECOLI Glucosamine-6-phosphate deaminase (Gene Name=nagB)

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