Structure of PDB 6q72 Chain A

Receptor sequence
>6q72A (length=386) Species: 1423 (Bacillus subtilis) [Search protein sequence]
MIKLCREVWIEVNLDAVKKNLRAIRRHIPHKSKIMAVVKANGYGHGSIEV
ARHALEHGASELAVASVEEGIVLRKAGITAPILVLGFTSLSCVKKSAAWN
ITLSAFQVDWMKEANEILEKEASANRLAIHINVDTGMGRLGVRTKEELLE
VVKALKASKFLRWTGIFTHFSTADEPDTTLTKLQHEKFISFLSFLKKQGI
ELPTVHMCNTAAAIAFPEFSADMIRLGIGLYGLYPSAYIKQLNLVKLEPA
LSLKARIAYVKTMRTEPRTVSYGATYIAEPNEVIATLPIGYADGYSRALS
NRGFVLHRGKRVPVAGRVTMDMIMVSLGENGEGKQGDEVVIYGKQKGAEI
SVDEVAEMLNTINYEVVSTLSRRIPRFYIRDGEIFK
3D structure
PDB6q72 Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K39 R139 H169 R225 Y272 T319 D321
Catalytic site (residue number reindexed from 1) K39 R139 H169 R225 Y272 T319 D321
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 K39 Y43 L85 H169 N209 T210 R225 G227 I228 Y364 K39 Y43 L85 H169 N209 T210 R225 G227 I228 Y364
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:6q72, PDBe:6q72, PDBj:6q72
PDBsum6q72
PubMed30977502
UniProtP94494|ALR2_BACSU Alanine racemase 2 (Gene Name=alr2)

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