Structure of PDB 5jzx Chain B

Receptor sequence
>5jzxB (length=327) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
FAGAHIAEAVPLAPLTTLRVGPIARRVITCTSAEQVVAALRHLDSADRPL
VFAGGSNLVIAENLTDLTVVRLANSGITIDGNLVRAEAGAVFDDVVVRAI
EQGLGGLECLSGIPGSAGATPVQNVGAYGAEVSDTITRVRLLDRCTGEVR
WVSARDLRFGYRTSVLKHADGLAVPTVVLEVEFALDPSGRSAPLRYGELI
AALNATSGERADPQAVREAVLALRARKGMVLDPTDHDTWSVGSFFTNPVV
TQDLAAGWLVERAGFGKGYPDAGAAPCRLSTKHALALTNRGGATAEDVVT
LARAVRDGVHDVFGITLKPEPVLIGCM
3D structure
PDB5jzx Crystal structure of UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) from Mycobacterium tuberculosis
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) R176 S257 E361
Catalytic site (residue number reindexed from 1) R162 S243 E320
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 B F66 A67 G68 G69 S70 N71 I127 P128 G129 S130 A133 V136 V139 G140 V191 V192 R238 S254 V255 G256 V363 F52 A53 G54 G55 S56 N57 I113 P114 G115 S116 A119 V122 V125 G126 V177 V178 R224 S240 V241 G242 V322
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:5jzx, PDBe:5jzx, PDBj:5jzx
PDBsum5jzx
PubMed29203374
UniProtP9WJL9|MURB_MYCTU UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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