Structure of PDB 1hsk Chain A

Receptor sequence
>1hskA (length=303) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
NKDIYQALQQLIPNEKIKVDEPLKRYTYTKTGGNADFYITPTKNEEVQAV
VKYAYQNEIPVTYLGNGSNIIIREGGIRGIVISLLSLDHIEVSDDAIIAG
SGAAIIDVSRVARDYALTGLEFACGIPGSIGGAVYMNAGAYGGEVKDCID
YALCVNEQGSLIKLTTKELELDYRNSIIQKEHLVVLEAAFTLAPGKMTEI
QAKMDDLTERRESKQPLEYPSCGSVFQRPPGHFAGKLIQDSNLQGHRIGG
VEVSTKHAGFMVNVDNGTATDYENLIHYVQKTVKEKFGIELNREVRIIGE
HPK
3D structure
PDB1hsk A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R188 S238 E308
Catalytic site (residue number reindexed from 1) R174 S224 E294
Enzyme Commision number 1.3.1.98: UDP-N-acetylmuramate dehydrogenase.
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 A Y42 Y77 G79 N80 G81 S82 N83 I84 P141 G142 S143 G146 A147 Y149 A152 G153 R188 V198 V199 R225 S235 F274 R310 Y28 Y63 G65 N66 G67 S68 N69 I70 P127 G128 S129 G132 A133 Y135 A138 G139 R174 V184 V185 R211 S221 F260 R296
Gene Ontology
Molecular Function
GO:0008762 UDP-N-acetylmuramate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1hsk, PDBe:1hsk, PDBj:1hsk
PDBsum1hsk
PubMed11327854
UniProtP61431|MURB_STAAU UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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