Structure of PDB 3e5p Chain B

Receptor sequence
>3e5pB (length=371) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
MVVGWHRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVE
SAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVDLAYVPLLIQY
DLSVTVATQEWLEAALQQLTPESNTPLRVHLKVDTGMGRIGFLTPEETKQ
AVRFVQSHKEFLWEGIFTHFSTADEIDTSYFEKQAGRFKAVLAVLEELPR
YVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSYALKPALRLT
SELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFTVL
VNGKRCEIVGRVCMDQCMIRLAEEVPVGPVVTLVGKDGNEENTLQMVAEK
LETIHYEVACTFSQRIPREYN
3D structure
PDB3e5p Structural insights into the alanine racemase from Enterococcus faecalis.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) K40 R139 H169 R222 Y267 C313 D315
Catalytic site (residue number reindexed from 1) K40 R139 H169 R222 Y267 C313 D315
Enzyme Commision number 5.1.1.1: alanine racemase.
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 PLP B K40 Y44 R139 H169 S207 G224 V225 Y356 K40 Y44 R139 H169 S207 G224 V225 Y356
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008784 alanine racemase activity
GO:0016853 isomerase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006522 alanine metabolic process
GO:0009252 peptidoglycan biosynthetic process
GO:0030632 D-alanine biosynthetic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:3e5p, PDBe:3e5p, PDBj:3e5p
PDBsum3e5p
PubMed19328247
UniProtQ837J0

[Back to BioLiP]