Structure of PDB 3int Chain A

Receptor sequence
>3intA (length=383) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
KSKKILIVGAGFSGAVIGRQLAEKGHQVHIIDQRDHIGGNSYDARDSETN
VMVHVYGPHIFHTDNETVWNYINKHAEMMPYVNRVKATVNGQVFSLPINL
HTINQFFSKTCSPDEARALIAEKGDSTIADPQTFEEQALRFIGKELYEAF
FKGYTIKQWGMQPSELPASILKRLPVRFNYDDNYFNHKFQGMPKCGYTQM
IKSILNHENIKVDLQREFIVDERTHYDHVFYSGPLDAFYGYQYGRLGYRT
LDFKKFIYQGDYQGCAVMNYCSVDVPYTRITEHKYFSPWEQHDGSVCYKE
YSRACEENDIPYYPIRQMGEMALLEKYLSLAENETNITFVGRLGTYRYLD
MDVTIAEALKTAEVYLNSLTDNQPMPVFTVSVG
3D structure
PDB3int X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin .
ChainA
Resolution2.51 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R174 R178 R250 R280 E301 Y349 D351
Catalytic site (residue number reindexed from 1) R173 R177 R249 R279 E300 Y348 D350
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 FDA A V9 G12 S14 D33 Q34 R35 G40 H60 I61 F219 G234 P235 Y313 Y314 R343 Y349 L350 D351 M352 T355 V8 G11 S13 D32 Q33 R34 G39 H59 I60 F218 G233 P234 Y312 Y313 R342 Y348 L349 D350 M351 T354
BS02 UDP A F152 Y155 T156 W160 Y185 N270 F151 Y154 T155 W159 Y184 N269
Gene Ontology
Molecular Function
GO:0008767 UDP-galactopyranose mutase activity

View graph for
Molecular Function
External links
PDB RCSB:3int, PDBe:3int, PDBj:3int
PDBsum3int
PubMed19719175
UniProtQ48485|GLF1_KLEPN UDP-galactopyranose mutase (Gene Name=rfbD)

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