Structure of PDB 2dkd Chain B

Receptor sequence
>2dkdB (length=535) Species: 5476 (Candida albicans) [Search protein sequence]
MSIEQTLSQYLPSHPKPQVTFTYGTAGFRMKADKLDYVTFTVGIIASLRS
KYLQGKTVGVMITASHNPPEDNGVKVVDPLGSMLESSWEKYATDLANASP
SPNSLVEVIKNLVSDLKIDLSIPANVVIARDSRESSPALSMATIDGFQSV
PNTKYQDFGLFTTPELHYVTRTLNDPDFGKPTEDGYYSKLAKSFQEIYTI
CESNNEKIDITIDAANGVGAPKIQELLEKYLHKEISFTVVNGDYKQPNLL
NFDCGADYVKTNQKLPKNVKPVNNKLYASFDGDADRLICYYQNNDNKFKL
LDGDKLSTLFALFLQQLFKQIDPTKISLNIGVVQTAYANGSSTKYVEDVL
KIPVRCTPTGVKHLHHEAENFDIGVYFEANGHGTVIFNPEAEKKIFDYKP
NNDNEAKAIKVLQNFSQLINQTVGDAISDLLAVLIVVHYLKLSPSDWDNE
YTDLPNKLVKVIVPDRSIFKTTNAERTLVEPKGMQDEIDKLVAQYPNGRS
FVRASGTEDAVRVYAEADTQNNVEELSKAVSELVK
3D structure
PDB2dkd Crystal Structures of N-Acetylglucosamine-phosphate Mutase, a Member of the {alpha}-D-Phosphohexomutase Superfamily, and Its Substrate and Product Complexes.
ChainB
Resolution2.1 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) S65 H66 K75
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 NG1 B Y346 E387 N389 R512 S514 G515 T516 R521 Y337 E378 N380 R503 S505 G506 T507 R512
BS02 PO4 B S66 H67 D294 R295 S65 H66 D285 R286
BS03 ZN B S66 D290 D292 D294 S65 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:2dkd, PDBe:2dkd, PDBj:2dkd
PDBsum2dkd
PubMed16651269
UniProtQ9P4V2|AGM1_CANAX Phosphoacetylglucosamine mutase (Gene Name=AGM1)

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