Structure of PDB 5j8x Chain A

Receptor sequence
>5j8xA (length=340) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYV
IGQAMKAGKFKETDLVTIGNMFLKPGMQVPVSQLIRGINLQSGNDACVAM
ADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDADGQYSSARDMALI
GQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTD
KAGYNLVASATEGQMRLISAVMGGRTFKGREAESKKLLTWGFRFFETVNP
LKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNSSE
LHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFF
3D structure
PDB5j8x Structural basis of metallo-beta-lactamase, serine-beta-lactamase and penicillin-binding protein inhibition by cyclic boronates.
ChainA
Resolution2.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L22 G28 L45 M48 M49 T50
Catalytic site (residue number reindexed from 1) L19 G25 L42 M45 M46 T47
Enzyme Commision number 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase.
3.5.2.6: beta-lactamase.
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 OK3 A S44 S110 L153 R198 T214 G215 H216 D218 R248 S41 S92 L135 R180 T196 G197 H198 D200 R230 PDBbind-CN: -logKd/Ki=8.80,IC50=0.0016uM
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008658 penicillin binding
GO:0008800 beta-lactamase activity
GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0000270 peptidoglycan metabolic process
GO:0006508 proteolysis
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005886 plasma membrane
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5j8x, PDBe:5j8x, PDBj:5j8x
PDBsum5j8x
PubMed27499424
UniProtP0AEB2|DACA_ECOLI D-alanyl-D-alanine carboxypeptidase DacA (Gene Name=dacA)

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