Structure of PDB 4ztc Chain A

Receptor sequence

>4ztcA (length=385) Species: 197 (Campylobacter jejuni)

MRFFLSPPHMGGNELKYIEEVFKSNYIAPLGEFVNRFEQSVKDYSKSENA
LALNSATAALHLALRVAGVKQDDIVLASSFTFIASVAPICYLKAKPVFID
CDETYNIDVDLLKLAIKECEKKPKALILTHLYGNAAKMDEIVEICKENDI
VLIEDAAEALGSFYKNKALGTFGEFGVYSYNGNAIITTSGGGMLIGKNKE
KIEKARFYSTQARENCLHYEHLDYGYNYRLSNVLGAIGVAQMEVLEQRVL
KKREIYEWYKEFLGEYFSFLDELENSRSNRWLSTALINFDKNELNSCQKD
INISQKNITLHPKISKLIEDLKNKQIETRPLWKTMHAQEVFKGAKAYLNG
NSELFFQKGICLPSGTAMSKDDVYEISKLILKSIK

3D structure

• PDB: 4ztc Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F82 D155 E158 N181 A184 Y219 R229
• Catalytic site (residue number reindexed from 1): F82 D155 E158 N181 A184 Y219 R229
• Enzyme Commision number: 2.6.1.34: UDP-N-acetylbacillosamine 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	4RA	A	F4 P8 A56 T57 F82 A84 D155 A157 E158 S179 N181 G182 N183 R329	F4 P8 A56 T57 F82 A84 D155 A157 E158 S179 N181 G182 N183 R329

Gene Ontology

Molecular Function

• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0047302 UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose transaminase activity

Biological Process

• GO:0000271 polysaccharide biosynthetic process
• GO:0006486 protein glycosylation

External links

• PDB: RCSB:4ztc, PDBe:4ztc, PDBj:4ztc
• PDBsum: 4ztc
• PubMed: 26178292
• UniProt: Q0P9D3|PGLE_CAMJE UDP-N-acetylbacillosamine transaminase (Gene Name=pglE)