Structure of PDB 4lut Chain B

Receptor sequence
>4lutB (length=364) Species: 272563 (Clostridioides difficile 630) [Search protein sequence]
KITVPTWAEINLDNLRFNLNNIKNLLEEDIKICGVIKADAYGHGAVEVAK
LLEKEKVDYLAVARTAEGIELRQNGITLPILNLGYTPDEAFEDSIKNKIT
MTVYSLETAQKINEIAKSLGEKACVHVKIDSGMTRIGFQPNEESVQEIIE
LNKLEYIDLEGMFTHFATADEVSKEYTYKQANNYKFMSDKLDEAGVKIAI
KHVSNSAAIMDCPDLRLNMVRAGIILYGHYPSDDVFKDRLELRPAMKLKS
KIGHIKQETIATVPIGYADGFTRIQKNPKVLIKGEVFDVVGRICMDQIMV
RIDKDIDIKVGDEVILFGEGEVTAERIAKDLGTINYEVLCMISRRVDRVY
MENNELVQINSYLL
3D structure
PDB4lut Structural and biochemical analyses of alanine racemase from the multidrug-resistant Clostridium difficile strain 630.
ChainB
Resolution2.26 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 R137 H167 R223 C314 D316
Catalytic site (residue number reindexed from 1) K37 R135 H165 R221 C294 D296
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 B Y287 M315 Y267 M295
BS02 DCS B K39 Y43 L85 R137 H167 S208 R223 G225 I226 Y356 K37 Y41 L83 R135 H165 S206 R221 G223 I224 Y336
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:4lut, PDBe:4lut, PDBj:4lut
PDBsum4lut
PubMed25004969
UniProtQ180W0

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