Structure of PDB 1dth Chain B

Receptor sequence
>1dthB (length=202) Species: 8730 (Crotalus atrox) [Search protein sequence]
QNLPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIH
VSLTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTA
IELDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGM
EHDGKDCLRGASLCIMRPGLTKGRSYEFSDDSMHYYERFLKQYKPQCILN
KP
3D structure
PDB1dth Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.42: atrolysin C.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B H142 H146 H152 H142 H146 H152
BS02 CA B E9 D93 C197 N200 E9 D93 C197 N200
BS03 BAT B L108 G109 V138 T139 H142 E143 H152 C164 I165 R167 P168 G169 L170 Y176 L108 G109 V138 T139 H142 E143 H152 C164 I165 R167 P168 G169 L170 Y176 MOAD: ic50=6nM
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
Biological Process
GO:0006508 proteolysis

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

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