Structure of PDB 1qf2 Chain A Binding Site BS06

Receptor Information
>1qf2 Chain A (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand IDTI3
InChIInChI=1S/C22H24N2O4S/c25-20(14-23-21(26)19(29)13-15-7-3-1-4-8-15)24-17(11-12-18(24)22(27)28)16-9-5-2-6-10-16/h1-10,17-19,29H,11-14H2,(H,23,26)(H,27,28)/t17-,18+,19+/m1/s1
InChIKeyZWDQTNWLXALTOV-QYZOEREBSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(N2C(C(=O)O)CCC2c1ccccc1)CNC(=O)C(S)Cc3ccccc3
OpenEye OEToolkits 1.5.0c1ccc(cc1)C[C@@H](C(=O)NCC(=O)N2[C@H](CC[C@H]2C(=O)O)c3ccccc3)S
CACTVS 3.341OC(=O)[CH]1CC[CH](N1C(=O)CNC(=O)[CH](S)Cc2ccccc2)c3ccccc3
CACTVS 3.341OC(=O)[C@@H]1CC[C@@H](N1C(=O)CNC(=O)[C@@H](S)Cc2ccccc2)c3ccccc3
OpenEye OEToolkits 1.5.0c1ccc(cc1)CC(C(=O)NCC(=O)N2C(CCC2C(=O)O)c3ccccc3)S
FormulaC22 H24 N2 O4 S
Name[(2S)-2-SULFANYL-3-PHENYLPROPANOYL]-GLY-(5-PHENYLPROLINE);
RB106
ChEMBLCHEMBL419499
DrugBankDB02669
ZINCZINC000006580513
PDB chain1qf2 Chain A Residue 317 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1qf2 Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases.
Resolution2.06 Å
Binding residue
(original residue number in PDB)		N112 F130 L133 V139 H142 E143 L202 R203 H231
Binding residue
(residue number reindexed from 1)		N112 F130 L133 V139 H142 E143 L202 R203 H231
Annotation score1
Binding affinityMOAD: Ki=1200nM
PDBbind-CN: -logKd/Ki=5.92,Ki=1200nM
Enzymatic activity
Catalytic site (original residue number in PDB) H142 E143 H146 Y157 E166 D226 H231
Catalytic site (residue number reindexed from 1) H142 E143 H146 Y157 E166 D226 H231
Enzyme Commision number 3.4.24.27: thermolysin.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1qf2, PDBe:1qf2, PDBj:1qf2
PDBsum1qf2
PubMed10504225
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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