Structure of PDB 3ukp Chain E

Receptor sequence
>3ukpE (length=509) Species: 746128 (Aspergillus fumigatus) [Search protein sequence]
THPDISVDVLVIGAGPTGLGAAKRLNQIDGPSWMIVDSNETPGGLASTDV
TPEGFLYDVGGHVIFSHYKYFDDCLDEALPKEDDWYTHQRISYVRCQGQW
VPYPFQNNISMLPKEEQVKCIDGMIDAALEARVANTKPKTFDEWIVRMMG
TGIADLFMRPYNFKVWAVPTTKMQCAWLGERVAAPNLKAVTTNVILGKTA
GNWGPNATFRFPARGGTGGIWIAVANTLPKEKTRFGEKGKVTKVNANNKT
VTLQDGTTIGYKKLVSTMAVDFLAEAMNDQELVGLTKQLFYSSTHVIGVG
VRGSRPERIGDKCWLYFPEDNCPFYAATIFSNYSPYNQPEASKKLPTMQL
ADGSRPQSTEAKEGPYWSIMLEVSESSMKPVNQETILADCIQGLVNTEML
KPTDEIVSTYHRRFDHGYPTPTLEREGALTQILPKLQDKDIWSRGRFGSW
RYEVGNQDHSFMLGVEAVDNIVNGAVELTLNYPDFVNGRQNTERRLVDGA
QVFAKSKAQ
3D structure
PDB3ukp Structural Insight into the Unique Substrate Binding Mechanism and Flavin Redox State of UDP-galactopyranose Mutase from Aspergillus fumigatus.
ChainE
Resolution3.1 Å
3D
structure
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Enzymatic activity
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 E I13 G14 G16 P17 T18 D38 S39 L46 H63 V64 M269 Y419 G446 R447 G456 N457 Q458 S461 I12 G13 G15 P16 T17 D37 S38 L45 H62 V63 M268 Y418 G445 R446 G455 N456 Q457 S460
BS02 GDU E Y104 M159 Y162 N163 V183 N207 W315 Y103 M158 Y161 N162 V182 N206 W314
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008767 UDP-galactopyranose mutase activity
GO:0016853 isomerase activity
Biological Process
GO:0071555 cell wall organization

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Molecular Function
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Biological Process
External links
PDB RCSB:3ukp, PDBe:3ukp, PDBj:3ukp
PDBsum3ukp
PubMed22334662
UniProtQ4W1X2|GLFA_ASPFM UDP-galactopyranose mutase (Gene Name=glfA)

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