Structure of PDB 1eeh Chain A

Receptor sequence

>1eehA (length=431) Species: 562 (Escherichia coli)

ADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAV
ERHTGSLNDEWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCR
EAQAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNIGLPALMLLDDE
CELYVLELSSFQLETTSSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLR
IYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHLTWLRVKGEKVL
NVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVV
LEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLA
RYLNGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDM
VLLSPACASLDQFKNFEQRGNEFARLAKELG

3D structure

• PDB: 1eeh Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K115 S116 N138 L147 H183
• Catalytic site (residue number reindexed from 1): K115 S116 N138 L147 H183
• Enzyme Commision number: 6.3.2.9: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase.

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	UMA	A	L15 T16 D35 T36 R37 P72 G73 G137 N138 F161	L15 T16 D35 T36 R37 P72 G73 G137 N138 F161

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0008764 UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
• GO:0016874 ligase activity
• GO:0016881 acid-amino acid ligase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0008360 regulation of cell shape
• GO:0009058 biosynthetic process
• GO:0009252 peptidoglycan biosynthetic process
• GO:0051301 cell division
• GO:0071555 cell wall organization

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1eeh, PDBe:1eeh, PDBj:1eeh
• PDBsum: 1eeh
• PubMed: 10966819
• UniProt: P14900|MURD_ECOLI UDP-N-acetylmuramoylalanine--D-glutamate ligase (Gene Name=murD)