Structure of PDB 1pwd Chain A

Receptor sequence
>1pwdA (length=345) Species: 31952 (Streptomyces sp. R61) [Search protein sequence]
LPAPDDTGLQAVLHTALSQGAPGAMVRVDDNGTIHQLSEGVADRATGRAI
TTTDRFRVGSVTKSFSAVVLLQLVDEGKLDLDASVNTYLPGLLPDDRITV
RQVMSHRSGLYDYTNDMFAQTVPGFESVRNKVFSYQDLITLSLKHGVTNA
PGAAYSYSNTNFVVAGMLIEKLTGHSVATEYQNRIFTPLNLTDTFYVHPD
TVIPGTHANGYLTPDEAGGALVDSTEQTVSWAQSAGAVISSTQDLDTFFS
ALMSGQLMSAAQLAQMQQWTTVNSTQGYGLGLRRRDLSCGISVYGHTGTV
QGYYTYAFASKDGKRSVTALANTSNNVNVLNTMARTLESAFCGKP
3D structure
PDB1pwd Crystal structures of complexes between the R61 DD-peptidase and peptidoglycan-mimetic beta-lactams: a non-covalent complex with a "perfect penicillin"
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S62 K65 D114 T116 V130 Y159 N161 V165 T227 H298 G304
Catalytic site (residue number reindexed from 1) S60 K63 D112 T114 V128 Y157 N159 V163 T225 H296 G302
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 0MU A S62 T116 F120 Y159 N161 W233 T299 G300 T301 S60 T114 F118 Y157 N159 W231 T297 G298 T299
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0008360 regulation of cell shape
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pwd, PDBe:1pwd, PDBj:1pwd
PDBsum1pwd
PubMed15581896
UniProtP15555|DAC_STRSR D-alanyl-D-alanine carboxypeptidase

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