Structure of PDB 1xqk Chain A Binding Site BS02

Receptor Information
>1xqk Chain A (length=382) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVA
RTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRI
ALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVAL
IERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHC
ANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRL
VHVKKLQPGEKVSFGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDG
QKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLET
INYEVPCTISYRVPRIFFRHKRIMEVRNAIGR
Ligand information
Ligand IDPMH
InChIInChI=1S/C11H14N3O7P/c1-6-10(15)8(3-13-9-5-20-14-11(9)16)7(2-12-6)4-21-22(17,18)19/h2,5,13,15H,3-4H2,1H3,(H,14,16)(H2,17,18,19)
InChIKeyPXWFNGNWQUPGPJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCc1c(c(O)c(nc1)C)CNc2conc2O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNc2conc2O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNc2conc2O)c1O
FormulaC11 H14 N3 O7 P
Name(5-HYDROXY-4-{[(3-HYDROXYISOXAZOL-4-YL)AMINO]METHYL}-6-METHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE;
PMP-HYDROXYISOXAZOLE;
PYRIDOXAMINE-5-PHOSPHATE-HYDROXYISOXAZOLE
ChEMBL
DrugBankDB03097
ZINCZINC000002046808
PDB chain1xqk Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1xqk Effect of a Y265F Mutant on the Transamination-Based Cycloserine Inactivation of Alanine Racemase
Resolution1.95 Å
Binding residue
(original residue number in PDB)		F265 M312
Binding residue
(residue number reindexed from 1)		F264 M311
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K39 R136 H166 R219 F265 C311 D313
Catalytic site (residue number reindexed from 1) K38 R135 H165 R218 F264 C310 D312
Enzyme Commision number 5.1.1.1: alanine racemase.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1xqk, PDBe:1xqk, PDBj:1xqk
PDBsum1xqk
PubMed15807525
UniProtP10724|ALR_GEOSE Alanine racemase (Gene Name=alr)

[Back to BioLiP]