Structure of PDB 2dy3 Chain B

Receptor sequence
>2dy3B (length=340) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
MNLLTTKIDLDAIAHNTRVLKQMAGPAKLMAVVKANAYNHGVEKVAPVIA
AHGADAFGVATLAEAMQLRDIGISQEVLCWIWTPEQDFRAAIDRNIDLAV
ISPAHAKALIETDAEHIRVSIKIDSGLHRSGVDEQEWEGVFSALAAAPHI
EVTGMFTHLACAPETDRQIIAFRRALALARKHGLECPVNHVCNSPAFLTR
SDLHMEMVRPGLAFYGLEPVAGLEHGLKPAMTWEAKVSVVKQIRGFVAVV
PAGYADGMPRHAQGKFSVTIDGLDYPQVGRVCMDQFVISLGDNPHGVEAG
AKAVIFGENGHDATDFAERLDTINYEVVCRPTGRTVRAYV
3D structure
PDB2dy3 Crystal Structure of Alanine Racemase from Corynebacterium glutamicum at 2.1 A resolution
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K34 R129 H158 R214 C303 D305
Catalytic site (residue number reindexed from 1) K34 R129 H158 R209 C282 D284
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 V32 K34 Y38 W80 H158 N198 S199 R214 P215 G216 L217 Y346 V32 K34 Y38 W80 H158 N193 S194 R209 P210 G211 L212 Y325
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2dy3, PDBe:2dy3, PDBj:2dy3
PDBsum2dy3
PubMed
UniProtQ8RSU9|ALR_CORGL Alanine racemase (Gene Name=alr)

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