Structure of PDB 2dkc Chain B

Receptor sequence
>2dkcB (length=535) Species: 5476 (Candida albicans) [Search protein sequence]
MSIEQTLSQYLPSHPKPQGVTFTYGTAGFRMKADKLDYVTFTVGIIASLR
SKYLQGKTVGVMITASHNPPEDNGVKVVDPLGSMLESSWEKYATDLANAS
PSPKNSLVEVIKNLVSDLKIDLSIPANVVIARDSRESSPALSMATIDGFQ
SVPNTKYQDFGLFTTPELHYVTRTLNDPDFGKPTEDGYYSKLAKSFQEIY
TICENEKIDITIDAANGVGAPKIQELLEKYLHKEISFTVVNGDYKQPNLL
NFDCGADYVKTNQKLPKNVKPVNNKLYASFDGDADRLICYYQNNDNKFKL
LDGDKLSTLFALFLQQLFKQIDPTKISLNIGVVQTAYANGSSTKYVEDVL
KIPVRCTPTGVKHLHHEAENFDIGVYFEANGHGTVIFNPEAEKKIFDYKP
NNDNEAKAIKVLQNFSQLINQTVGDAISDLLAVLIVVHYLKLSPSDWDNE
YTDLPNKLVKVIVPDRSIFKTTNAERTLVEPKGMQDEIDKLVAQYPNGRS
FVRASGTEDAVRVYAEADTQNNVEELSKAVSELVK
3D structure
PDB2dkc Crystal Structures of N-Acetylglucosamine-phosphate Mutase, a Member of the {alpha}-D-Phosphohexomutase Superfamily, and Its Substrate and Product Complexes.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S66 H67 K76
Catalytic site (residue number reindexed from 1) S66 H67 K76
Enzyme Commision number 5.4.2.3: phosphoacetylglucosamine 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 16G B T26 T368 G369 V370 E387 H391 R512 S514 T516 R521 T26 T359 G360 V361 E378 H382 R503 S505 T507 R512
BS02 PO4 B R30 S66 H67 R295 H391 R30 S66 H67 R286 H382
BS03 ZN B S66 D290 D292 D294 S66 D281 D283 D285
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004610 phosphoacetylglucosamine mutase activity
GO:0016853 isomerase activity
GO:0016868 intramolecular phosphotransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006031 chitin biosynthetic process
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
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Biological Process
External links
PDB RCSB:2dkc, PDBe:2dkc, PDBj:2dkc
PDBsum2dkc
PubMed16651269
UniProtQ9P4V2|AGM1_CANAX Phosphoacetylglucosamine mutase (Gene Name=AGM1)

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