Structure of PDB 3inr Chain B

Receptor sequence

>3inrB (length=378) Species: 573 (Klebsiella pneumoniae)

KSKKILIVGAGFSGAVIGRQLAEKGHQVHIIDQRDHIGGNSYDARDSETN
VMVHVYGPHIFHTDNETVWNYINKHAEMMPYVNRVKATVNGQVFSLPINL
HTINQFFSKTCSPDEARALIAEKGDSTTFEEQALRFIGKELYEAFFKGYT
IKQWGMQPSELPASILKRLPVRFNYDDNYFNHKFQGMPKCGYTQMIKSIL
NHENIKVDLQREFIVDERTHYDHVFYSGPLDAFYGYQYGRLGYRTLDFKK
FIYQGDYQGCAVMNYCSVDVPYTRITEHKYFSPWEQHDGSVCYKEYSRAC
EENDIPYYPIRQMGEMALLEKYLSLAENETNITFVGRLGTYRYLDMDVTI
AEALKTAEVYLNSLTDNQPMPVFTVSVG

3D structure

• PDB: 3inr X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin .
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R174 R178 R250 R280 E301 Y349 D351
• Catalytic site (residue number reindexed from 1): R168 R172 R244 R274 E295 Y343 D345
• Enzyme Commision number: 5.4.99.9: UDP-galactopyranose mutase.

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	FAD	B	V9 G10 G12 S14 D33 Q34 G40 P59 H60 I61 F219 G234 Y313 R343 Y349 L350 D351 M352 T355	V8 G9 G11 S13 D32 Q33 G39 P58 H59 I60 F213 G228 Y307 R337 Y343 L344 D345 M346 T349
BS02	GDU	B	F151 F152 Y155 T156 W160 R174 L175 Y185 Y314 Y349 D351	F145 F146 Y149 T150 W154 R168 L169 Y179 Y308 Y343 D345

Gene Ontology

Molecular Function

• GO:0008767 UDP-galactopyranose mutase activity

External links

• PDB: RCSB:3inr, PDBe:3inr, PDBj:3inr
• PDBsum: 3inr
• PubMed: 19719175
• UniProt: Q48485|GLF1_KLEPN UDP-galactopyranose mutase (Gene Name=rfbD)