Structure of PDB 5fbz Chain A Binding Site BS03
Receptor Information
>5fbz Chain A (length=433) Species:
79882
(Sutcliffiella halmapala) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
NDVARGIVKADVAQNNFGLYGQGQIVAVADTGLDTGRNDSSMHEAFRGKI
TALYALGRTNNANDPNGHGTHVAGSVLGNATNKGMAPQANLVFQSIMDSG
GGLGGLPANLQTLFSQAYSAGARIHTNSWGAPVNGAYTTDSRNVDDYVRK
NDMTILFAAGNEGPGSGTISAPGTAKNAITVGATENLRPSFGSYADNINH
VAQFSSRGPTRDGRIKPDVMAPGTYILSARSSLAPDSSFWANHDSKYAYM
GGTSMATPIVAGNVAQLREHFVKNRGVTPKPSLLKAALIAGAADVGLGFP
NGNQGWGRVTLDKSLNVAFVNETSPLSTSQKATYSFTAQAGKPLKISLVW
SDAPGSTTASLTLVNDLDLVITAPNGTKYVGNDFTAPYDNNWDGRNNVEN
VFINAPQSGTYTVEVQAYNVPVGPQTFSLAIVH
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
5fbz Chain A Residue 602 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure 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
]
PDB
5fbz
Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
D366 L367 D368 D393 E399
Binding residue
(residue number reindexed from 1)
D366 L367 D368 D393 E399
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D30 H68 N161 S254
Catalytic site (residue number reindexed from 1)
D30 H68 N161 S254
Enzyme Commision number
3.4.21.14
: Transferred entry: 3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67.
Gene Ontology
Molecular Function
GO:0004252
serine-type endopeptidase activity
GO:0008236
serine-type peptidase activity
GO:0046872
metal ion binding
Biological Process
GO:0006508
proteolysis
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:5fbz
,
PDBe:5fbz
,
PDBj:5fbz
PDBsum
5fbz
PubMed
UniProt
A0A182DWC7
[
Back to BioLiP
]