Structure of PDB 4zah Chain G

Receptor sequence
>4zahG (length=367) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
HMIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKV
LLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD
VRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFV
VEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKAL
IERAEIIREKGTNRYTWRDIGSSYLMSDLQAAYLWAQLEAADRINQQRLA
LWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALINF
LKEAEIMAVFHYIPLHGCPAGEHFGEFHGEDRYTTKESERLLRLPLFYNL
SPVNQRTVIATLLNYFS
3D structure
PDB4zah Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.
ChainG
Resolution2.24 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F81 D152 Q155 H178 K181 R213 Y224 L234
Catalytic site (residue number reindexed from 1) F82 D153 Q156 H179 K182 R214 Y215 L225
Enzyme Commision number 2.6.1.59: dTDP-4-amino-4,6-dideoxygalactose transaminase.
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 T5K G S54 C55 T56 F81 D152 A154 Q155 S176 H178 K181 V318 H320 Y321 S55 C56 T57 F82 D153 A155 Q156 S177 H179 K182 V309 H311 Y312
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016740 transferase activity
GO:0019180 dTDP-4-amino-4,6-dideoxygalactose transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0009246 enterobacterial common antigen biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4zah, PDBe:4zah, PDBj:4zah
PDBsum4zah
PubMed26023720
UniProtP27833|WECE_ECOLI dTDP-4-amino-4,6-dideoxygalactose transaminase (Gene Name=wecE)

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