Structure of PDB 1dth Chain B Binding Site BS01

Receptor Information
>1dth Chain B (length=202) Species: 8730 (Crotalus atrox) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIH
VSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTA
IELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGM
EHDGKDCLRGASLCIMRPGLTKGRSYEFSDDSMHYYERFLKQYKPQCILN
KP
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1dth Chain B Residue 902 [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]
PDB1dth Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H142 H146 H152
Binding residue
(residue number reindexed from 1)		H142 H146 H152
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.24.42: atrolysin C.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1dth, PDBe:1dth, PDBj:1dth
PDBsum1dth
PubMed8610113
UniProtP15167|VM1AD_CROAT Snake venom metalloproteinase atrolysin-D

[Back to BioLiP]