Structure of PDB 1t31 Chain A Binding Site BS02

Receptor Information
>1t31 Chain A (length=226) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRS
ITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKAS
LTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMD
PQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGAAQGIVSYGR
SDAKPPAVFTRISHYQPWINQILQAN
Ligand information
Ligand IDOHH
InChIInChI=1S/C40H35N2O6P/c1-41(32-19-21-42(22-20-32)39(44)31-18-17-26-9-2-3-11-28(26)23-31)40(45)36-25-30-13-5-4-12-29(30)24-35(36)37(43)38(49(46,47)48)34-16-8-14-27-10-6-7-15-33(27)34/h2-18,23-25,32,38H,19-22H2,1H3,(H2,46,47,48)/t38-/m1/s1
InChIKeyXUJQPDQURBZEGJ-KXQOOQHDSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CN(C1CCN(CC1)C(=O)c2ccc3ccccc3c2)C(=O)c4cc5ccccc5cc4C(=O)C(c6cccc7c6cccc7)P(=O)(O)O
OpenEye OEToolkits 1.5.0CN(C1CCN(CC1)C(=O)c2ccc3ccccc3c2)C(=O)c4cc5ccccc5cc4C(=O)[C@@H](c6cccc7c6cccc7)P(=O)(O)O
CACTVS 3.341CN(C1CCN(CC1)C(=O)c2ccc3ccccc3c2)C(=O)c4cc5ccccc5cc4C(=O)[CH](c6cccc7ccccc67)[P](O)(O)=O
ACDLabs 10.04O=C(c2cc1ccccc1cc2)N7CCC(N(C(=O)c6cc3ccccc3cc6C(=O)C(c5c4ccccc4ccc5)P(=O)(O)O)C)CC7
CACTVS 3.341CN(C1CCN(CC1)C(=O)c2ccc3ccccc3c2)C(=O)c4cc5ccccc5cc4C(=O)[C@@H](c6cccc7ccccc67)[P](O)(O)=O
FormulaC40 H35 N2 O6 P
Name2-[3-({METHYL[1-(2-NAPHTHOYL)PIPERIDIN-4-YL]AMINO}CARBONYL)-2-NAPHTHYL]-1-(1-NAPHTHYL)-2-OXOETHYLPHOSPHONIC ACID
ChEMBL
DrugBankDB04016
ZINCZINC000024666930
PDB chain1t31 Chain A Residue 901 [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]
PDB1t31 A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		K40 H57 A190 F191 K192 G193 S195 S214 Y215 G216 R217 A226
Binding residue
(residue number reindexed from 1)		K28 H45 A177 F178 K179 G180 S182 S197 Y198 G199 R200 A207
Annotation score1
Binding affinityMOAD: Ki=2.3nM
PDBbind-CN: -logKd/Ki=8.64,Ki=2.3nM
BindingDB: Ki=2.3nM,IC50=4.5nM
Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 K192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H45 D89 K179 G180 D181 S182 G183
Enzyme Commision number 3.4.21.39: chymase.
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0042277 peptide binding
Biological Process
GO:0002003 angiotensin maturation
GO:0006508 proteolysis
GO:0006518 peptide metabolic process
GO:0016485 protein processing
GO:0022617 extracellular matrix disassembly
GO:0030163 protein catabolic process
GO:0030901 midbrain development
GO:0034769 basement membrane disassembly
GO:0045766 positive regulation of angiogenesis
GO:0050727 regulation of inflammatory response
GO:0071333 cellular response to glucose stimulus
GO:0140447 cytokine precursor processing
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0030141 secretory granule
GO:0036464 cytoplasmic ribonucleoprotein granule
GO:0043231 intracellular membrane-bounded organelle
GO:0062023 collagen-containing extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1t31, PDBe:1t31, PDBj:1t31
PDBsum1t31
PubMed15741158
UniProtP23946|CMA1_HUMAN Chymase (Gene Name=CMA1)

[Back to BioLiP]