Structure of PDB 1zvj Chain A Binding Site BS01

Receptor Information
>1zvj Chain A (length=354) Species: 192387 (Alicyclobacillus sendaiensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGVPA
PQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAPNT
DAGFLDAITTAIHDPTLKPSVVSISWGGPEDSWTSAAIAAMNRAFLDAAA
LGVTVLAAAGNSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASGGRIA
QETVWNDGPDGGATGGGVSRIFPLPAWQEHANVPPSANPGASSGRGVPDL
AGNADPATGYEVVIDGEATVIGGTSAVAPLFAALVARINQKLGKAVGYLN
PTLYQLPADVFHDITEGNNDIANRAQIYQAGPGWDPCTGLGSPIGVRLLQ
ALLP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1zvj Chain A Residue 401 [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]
PDB1zvj Processing, catalytic activity and crystal structures of kumamolisin-As with an engineered active site.
Resolution2.03 Å
Binding residue
(original residue number in PDB)
D316 I317 G334 G336 D338 L356 P357
Binding residue
(residue number reindexed from 1)
D313 I314 G331 G333 D335 L353 P354
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E78 D82 N164 S278
Catalytic site (residue number reindexed from 1) E75 D79 N161 S275
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1zvj, PDBe:1zvj, PDBj:1zvj
PDBsum1zvj
PubMed16704427
UniProtQ8GB88

[Back to BioLiP]