Structure of PDB 3bec Chain A

Receptor sequence
>3becA (length=352) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
NIKTMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYV
IGQAMKAGKFKETDLVTIGNDAWATGNPVFKGSSLMFLKPGMQVPVSQLI
RGINLQSGNDACVAMADFAAGSQDAFVGLMNSYVNALGLKNTHFQTVHGL
DADGQYSSARDMALIGQALIRDVPNEYSIYKEKEFTFNGIRQLNRNGLLW
DNSLNVDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGRTFKGREAESK
KLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG
RMKDLKASYVLNSSELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIP
EG
3D structure
PDB3bec Crystal structures of complexes of bacterial DD-peptidases with peptidoglycan-mimetic ligands: the substrate specificity puzzle
ChainA
Resolution1.6 Å
3D
structure
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Enzymatic activity
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 HJ2 A S44 R198 T214 G215 H216 R248 S41 R195 T211 G212 H213 R245
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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Cellular Component
External links
PDB RCSB:3bec, PDBe:3bec, PDBj:3bec
PDBsum3bec
PubMed18602645
UniProtP0AEB2|DACA_ECOLI D-alanyl-D-alanine carboxypeptidase DacA (Gene Name=dacA)

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