Structure of PDB 1niu Chain A

Receptor sequence
>1niuA (length=382) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVA
RTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRI
ALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVAL
IERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC
ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRL
VHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDG
QKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLET
INYEVPCTISYRVPRIFFRHKRIMEVRNAIGR
3D structure
PDB1niu A side reaction of alanine racemase: transamination of cycloserine.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K39 R136 H166 R219 Y265 C311 D313
Catalytic site (residue number reindexed from 1) K38 R135 H165 R218 Y264 C310 D312
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 DCS A K39 Y43 L85 R136 H166 S204 R219 G221 I222 Y354 K38 Y42 L84 R135 H165 S203 R218 G220 I221 Y353 MOAD: Ki=0.08uM
BS02 DCS A Y265 C311 M312 Y264 C310 M311 MOAD: Ki=0.08uM
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:1niu, PDBe:1niu, PDBj:1niu
PDBsum1niu
PubMed12741835
UniProtP10724|ALR_GEOSE Alanine racemase (Gene Name=alr)

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