Structure of PDB 4opn Chain B Binding Site BS01

Receptor Information
>4opn Chain B (length=174) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLL
QKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTE
DDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM
KGLAFIQDPDGYWIEILNPNKIAT
Ligand information
Ligand IDZBF
InChIInChI=1S/C20H24N4O8/c1-2-12-4-3-5-13(10-12)24(32)17(26)9-7-15(19(29)22-11-18(27)28)23-16(25)8-6-14(21)20(30)31/h1,3-5,10,14-15,32H,6-9,11,21H2,(H,22,29)(H,23,25)(H,27,28)(H,30,31)/t14-,15-/m0/s1
InChIKeyDNHXPPJCZZCCCC-GJZGRUSLSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C#Cc1cccc(c1)N(C(=O)CCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)O
CACTVS 3.385N[CH](CCC(=O)N[CH](CCC(=O)N(O)c1cccc(c1)C#C)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.385N[C@@H](CCC(=O)N[C@@H](CCC(=O)N(O)c1cccc(c1)C#C)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.7.6C#Cc1cccc(c1)N(C(=O)CC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)O
ACDLabs 12.01O=C(O)C(N)CCC(=O)NC(C(=O)NCC(=O)O)CCC(=O)N(O)c1cc(C#C)ccc1
FormulaC20 H24 N4 O8
NameL-gamma-glutamyl-N-(3-ethynylphenyl)-N-hydroxy-L-glutaminylglycine
ChEMBLCHEMBL4436073
DrugBank
ZINCZINC000210264517
PDB chain4opn Chain A Residue 202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4opn Reversible Inhibition of Glyoxalase I: Synthesis and Activity Evaluation
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Q34 R38 F68 L70 F93 E100 T102 N104
Binding residue
(residue number reindexed from 1)		Q26 R30 F60 L62 F85 E92 T94 N96
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) Q34 E100 H127 E173
Catalytic site (residue number reindexed from 1) Q26 E92 H119 E165
Enzyme Commision number 4.4.1.5: lactoylglutathione lyase.
Gene Ontology
Molecular Function
GO:0004462 lactoylglutathione lyase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006749 glutathione metabolic process
GO:0009438 methylglyoxal metabolic process
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
GO:0030316 osteoclast differentiation
GO:0043066 negative regulation of apoptotic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4opn, PDBe:4opn, PDBj:4opn
PDBsum4opn
PubMed
UniProtQ9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)

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