Structure of PDB 2mbr Chain A

Receptor sequence
>2mbrA (length=340) Species: 562 (Escherichia coli) [Search protein sequence]
HSLKPWNTFGIDHNAQHIVCAEDEQQLLNAWQYATAEGQPVLILGEGSNV
LFLEDYRGTVIINRIKGIEIHDEPDAWYLHVGAGENWHRLVKYTLQEGMP
GLENLALIPGCVGSSPIQNIGAYGVELQRVCAYVDSVELATGKQVRLTAK
ECRFGYRDSIFKHEYQDRFAIVAVGLRLPKEWQPVLTYGDLTRLDPTTVT
PQQVFNAVCHMRTTKLPDPKVNGNAGSFFKNPVVSAETAKALLSQFPTAP
NYPQADGSVKLAAGWLIDQCQLKGMQIGGAAVHRQQALVLINEDNAKSED
VVQLAHHVRQKVGEKFNVWLEPEVRFIGASGEVSAVETIS
3D structure
PDB2mbr X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R159 S229 E325
Catalytic site (residue number reindexed from 1) R157 S227 E323
Enzyme Commision number 1.3.1.98: UDP-N-acetylmuramate dehydrogenase.
Interaction with ligand
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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Biological Process
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Cellular Component
External links
PDB RCSB:2mbr, PDBe:2mbr, PDBj:2mbr
PDBsum2mbr
PubMed9020778
UniProtP08373|MURB_ECOLI UDP-N-acetylenolpyruvoylglucosamine reductase (Gene Name=murB)

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