Structure of PDB 3tx1 Chain A

Receptor sequence
>3tx1A (length=295) Species: 1639 (Listeria monocytogenes) [Search protein sequence]
MNNLQTKFPHIAIKLNEPLSKYTYTKTGGAADVFVMPKTIEEAQEVVAYC
HQNKIPLTILGNGSNLIIKDGGIRGVILHLDLLQTIERNNTQIVAMSGAK
LIDTAKFALNESLSGLEFACGIPGSIGGALHMNAGAYGGEISDVLEAATV
LTQTGELKKLKRSELKYRSTIAEKNYIVLDATFSLALEEKNLIQAKMDEL
TAAREAKQPLEYPSCGSVFKRPPGHFAGKLIQDSGLQGHIIGGAQVSLKH
AGFIVNIGGATATDYMNLIAYVQQTVREKFDVELETEVKIIGEDK
3D structure
PDB3tx1 X-ray crystal structure of Listeria monocytogenes EGD-e UDP-N-acetylenolpyruvylglucosamine reductase (MurB).
ChainA
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R170 S220 E290
Catalytic site (residue number reindexed from 1) R168 S217 E287
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 Y24 I59 G61 N62 G63 S64 N65 L66 I122 P123 G124 S125 G127 G128 A129 H131 A134 G135 R170 V181 R207 S217 C218 G219 Y24 I59 G61 N62 G63 S64 N65 L66 I122 P123 G124 S125 G127 G128 A129 H131 A134 G135 R168 V178 R204 S214 C215 G216
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:3tx1, PDBe:3tx1, PDBj:3tx1
PDBsum3tx1
PubMed
UniProtQ8Y776|MURB_LISMO UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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