Structure of PDB 3e5p Chain A

Receptor sequence
>3e5pA (length=370) Species: 1351 (Enterococcus faecalis) [Search protein sequence]
VVGWHRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVES
AKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVDLAYVPLLIQYD
LSVTVATQEWLEAALQQLTPESNTPLRVHLKVDTGMGRIGFLTPEETKQA
VRFVQSHKEFLWEGIFTHFSTADEIDTSYFEKQAGRFKAVLAVLEELPRY
VHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSYALKPALRLTS
ELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFTVLV
NGKRCEIVGRVCMDQCMIRLAEEVPVGPVVTLVGKDGNEENTLQMVAEKL
ETIHYEVACTFSQRIPREYN
3D structure
PDB3e5p Structural insights into the alanine racemase from Enterococcus faecalis.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K40 R139 H169 R222 Y267 C313 D315
Catalytic site (residue number reindexed from 1) K39 R138 H168 R221 Y266 C312 D314
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 A V38 K40 Y44 L86 H169 S207 R222 G224 V225 Y356 V37 K39 Y43 L85 H168 S206 R221 G223 V224 Y355
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

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Biological Process
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Cellular Component
External links
PDB RCSB:3e5p, PDBe:3e5p, PDBj:3e5p
PDBsum3e5p
PubMed19328247
UniProtQ837J0

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