Structure of PDB 3ukp Chain C

Receptor sequence
>3ukpC (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.
ChainC
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 C G14 G16 P17 T18 D38 S39 L46 A47 H63 V64 G240 V242 M269 R447 G456 N457 Q458 G13 G15 P16 T17 D37 S38 L45 A46 H62 V63 G239 V241 M268 R446 G455 N456 Q457
BS02 GDU C Y104 F158 M159 Y162 N163 R182 W315 Y453 N457 Y103 F157 M158 Y161 N162 R181 W314 Y452 N456
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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