Structure of PDB 3itb Chain C

Receptor sequence
>3itbC (length=347) Species: 562 (Escherichia coli) [Search protein sequence]
VEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALK
ADKIKLTDMVTVGKDAWATGNPALRGSSVMFLKPGDQVSVADLNKGVIIQ
SGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAPGQF
STARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNV
DGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWG
FRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLK
ASYTLTEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGG
3D structure
PDB3itb Crystal structures of penicillin-binding protein 6 from Escherichia coli.
ChainC
Resolution1.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase.
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 peptide C A39 S40 G81 S82 S83 S106 G148 R194 T210 G211 T212 A34 S35 G76 S77 S78 S101 G143 R189 T205 G206 T207
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0008233 peptidase activity
GO:0008658 penicillin binding
GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0006508 proteolysis
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0009410 response to xenobiotic stimulus
GO:0071555 cell wall organization
Cellular Component
GO:0005886 plasma membrane
GO:0030288 outer membrane-bounded periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3itb, PDBe:3itb, PDBj:3itb
PDBsum3itb
PubMed19807181
UniProtP08506|DACC_ECOLI D-alanyl-D-alanine carboxypeptidase DacC (Gene Name=dacC)

[Back to BioLiP]