Structure of PDB 1qin Chain B Binding Site BS01

Receptor Information
>1qin Chain B (length=176) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLI
QKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTE
DDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM
KGLAFIQDPDGYWIEILNPNKMATLM
Ligand information
Ligand IDGIP
InChIInChI=1S/C17H23IN4O8S/c18-9-1-3-10(4-2-9)22(30)17(29)31-8-12(15(26)20-7-14(24)25)21-13(23)6-5-11(19)16(27)28/h1-4,11-12,17,29-30H,5-8,19H2,(H,20,26)(H,21,23)(H,24,25)(H,27,28)/t11-,12-,17+/m0/s1
InChIKeySCHAHXXLASZJCD-NVGCLXPQSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCC(=O)N[CH](CS[CH](O)N(O)c1ccc(I)cc1)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CS[C@@H](O)N(O)c1ccc(I)cc1)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0c1cc(ccc1N(C(O)SC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)O)I
ACDLabs 10.04Ic1ccc(N(O)C(O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)cc1
OpenEye OEToolkits 1.5.0c1cc(ccc1N(C(O)SCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)O)I
FormulaC17 H23 I N4 O8 S
NameS-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE
ChEMBL
DrugBankDB03330
ZINCZINC000014880713
PDB chain1qin Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1qin Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Q33 R37 F67 L69 F71 E99 T101 N103
Binding residue
(residue number reindexed from 1)		Q26 R30 F60 L62 F64 E92 T94 N96
Annotation score2
Binding affinityMOAD: Ki=10nM
PDBbind-CN: -logKd/Ki=8.00,Ki=10nM
Enzymatic activity
Catalytic site (original residue number in PDB) Q33 E99 H126 E172
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:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006749 glutathione metabolic process
GO:0009438 methylglyoxal metabolic process
GO:0030316 osteoclast differentiation
GO:0043066 negative regulation of apoptotic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qin, PDBe:1qin, PDBj:1qin
PDBsum1qin
PubMed10521255
UniProtQ04760|LGUL_HUMAN Lactoylglutathione lyase (Gene Name=GLO1)

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