Structure of PDB 1dbi Chain A

Receptor sequence
>1dbiA (length=271) Species: 268807 (Bacillus sp. Ak1) [Search protein sequence]
WTPNDTYYQGYQYGPQNTYTDYAWDVTKGSSGQEIAVIDTGVDYTHPDLD
GKVIKGYDFVDNDYDPMDLNNHGTHVAGIAAAETNNATGIAGMAPNTRIL
AVRALDRNGSGTLSDIADAIIYAADSGAEVINLSLGCDCHTTTLENAVNY
AWNKGSVVVAAAGNNSYENVIAVGAVDQYDRLASFSNYGTWVDVVAPGVD
IVSTITGNRYAYMSGTSMASPHVAGLAALLASQGRNNIEIRQAIEQTADK
ISGTGTYFKYGRINSYNAVTY
3D structure
PDB1dbi Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D39 H72 N164 S226
Catalytic site (residue number reindexed from 1) D39 H72 N164 S217
Enzyme Commision number 3.4.21.-
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 CA A D5 D48 E83 N86 T88 I90 D5 D48 E83 N86 T88 I90
BS02 CA A D58 D63 D65 D58 D63 D65
BS03 CA A P47 D50 E83 P47 D50 E83
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1dbi, PDBe:1dbi, PDBj:1dbi
PDBsum1dbi
PubMed10588904
UniProtQ45670|THES_BACSJ Thermophilic serine proteinase

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