Structure of PDB 1atl Chain A

Receptor sequence
>1atlA (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).
ChainA
Resolution1.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 A H142 H146 H152 H140 H144 H150
BS02 CA A E9 D93 C197 N200 E7 D91 C195 N198
BS03 0QI A 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1atl, PDBe:1atl, PDBj:1atl
PDBsum1atl
PubMed8078901
UniProtP15167|VM1AD_CROAT Snake venom metalloproteinase atrolysin-D

[Back to BioLiP]