Structure of PDB 1atl Chain B

Receptor sequence
>1atlB (length=200) Species: 8730 (Crotalus atrox) [Search protein sequence]
LPQRYIELVVVADHRVFMKYNSDLNTIRTRVHEIVNFINGFYRSLNIHVS
LTDLEIWSNEDQINIQSASSDTLNAFAEWRETDLLNRKSHDNAQLLTAIE
LDEETLGLAPLGTMCDPKLSIGIVQDHSPINLLMGVTMAHELGHNLGMEH
DGKDCLRGASLCIMRPGLTKGRSYEFSDDSMHYYERFLKQYKPQCILNKP
3D structure
PDB1atl Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
ChainB
Resolution1.8 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 H140 H144 H150
BS02 CA B E9 D93 C197 N200 E7 D91 C195 N198
BS03 0QI B T107 L108 G109 H142 E143 H152 I165 R167 P168 G169 L170 T105 L106 G107 H140 E141 H150 I163 R165 P166 G167 L168 MOAD: Ki=0.52uM
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:1atl, PDBe:1atl, PDBj:1atl
PDBsum1atl
PubMed8078901
UniProtP15167|VM1AD_CROAT Snake venom metalloproteinase atrolysin-D

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