Structure of PDB 4zah Chain H

Receptor sequence

>4zahH (length=368) Species: 83333 (Escherichia coli K-12)

HMIPFNAPPVVGTELDYMQSAMGSGKLCGDGGFTRRCQQWLEQRFGSAKV
LLTPSCTASLEMAALLLDIQPGDEVIMPSYTFVSTANAFVLRGAKIVFVD
VRPDTMNIDETLIEAAITDKTRVIVPVHYAGVACEMDTIMALAKKHNLFV
VEDAAQGVMSTYKGRALGTIGHIGCFSFHETKNYTAGGEGGATLINDKAL
IERAEIIREKGTNRSYTWRDIGSSYLMSDLQAAYLWAQLEAADRINQQRL
ALWQNYYDALAPLAKAGRIELPSIPDGCVQNAHMFYIKLRDIDDRSALIN
FLKEAEIMAVFHYIPLHGCPAGEHFGEFHGEDRYTTKESERLLRLPLFYN
LSPVNQRTVIATLLNYFS

3D structure

• PDB: 4zah Structural Basis for the Stereochemical Control of Amine Installation in Nucleotide Sugar Aminotransferases.
• Chain: H
• Resolution: 2.24 Å

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 Y216 L226
• 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	H	R213 Y224	R214 Y216
BS02	T5K	H	S54 C55 T56 F81 D152 A154 Q155 S176 H178 K181 V318 F319 H320 Y321	S55 C56 T57 F82 D153 A155 Q156 S177 H179 K182 V310 F311 H312 Y313

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

External links

• PDB: RCSB:4zah, PDBe:4zah, PDBj:4zah
• PDBsum: 4zah
• PubMed: 26023720
• UniProt: P27833|WECE_ECOLI dTDP-4-amino-4,6-dideoxygalactose transaminase (Gene Name=wecE)