Structure of PDB 3ukk Chain C

Receptor sequence
>3ukkC (length=516) Species: 746128 (Aspergillus fumigatus) [Search protein sequence]
THPDISVDVLVIGAGPTGLGAAKRLNQIDGPSWMIVDSNETPGGLASTDV
TPEGFLYDVGGHVIFSHYKYFDDCLDEALPKEDDWYTHQRISYVRCQGQW
VPYPFQNNISMLPKEEQVKCIDGMIDAALEARVANTKPKTFDEWIVRMMG
TGIADLFMRPYNFKVWAVPTTKMQCAWLGEKVAAPNLKAVTTNVILGKTA
GNWGPNATFRFPARGGTGGIWIAVANTLPKEKTRFGEKGKVTKVNANNKT
VTLQDGTTIGYKKLVSTMAVDFLAEAMNDQELVGLTKQLFYSSTHVIGVG
VRGSRPERIGDKCWLYFPEDNCPFYRATIFSNYSPYNQPEASKKLPTMQL
ADGSRPQSTEAKEGPYWSIMLEVSESSMKPVNQETILADCIQGLVNTEML
KPTDEIVSTYHRRFDHGYPTPTLEREGALTQILPKLQDKDIWSRGRFGSW
RYEVGNQDHSFMLGVEAVDNIVNGAVELTLNYPDFVNGRQNTERRLVDGA
QVFAKSKAQLEHHHHH
3D structure
PDB3ukk Structural Insight into the Unique Substrate Binding Mechanism and Flavin Redox State of UDP-galactopyranose Mutase from Aspergillus fumigatus.
ChainC
Resolution2.75 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 G16 T18 D38 S39 L46 V60 H63 K241 V242 M269 G446 R447 N457 Q458 S461 G15 T17 D37 S38 L45 V59 H62 K240 V241 M268 G445 R446 N456 Q457 S460
BS02 UDP C Y104 F158 M159 N163 K182 V183 R327 Y453 Y103 F157 M158 N162 K181 V182 R326 Y452
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:3ukk, PDBe:3ukk, PDBj:3ukk
PDBsum3ukk
PubMed22334662
UniProtQ4W1X2|GLFA_ASPFM UDP-galactopyranose mutase (Gene Name=glfA)

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