Structure of PDB 1a2q Chain A

Receptor sequence
>1a2qA (length=275) Species: 1390 (Bacillus amyloliquefaciens) [Search protein sequence]
AQSVPYGVSQIKAPALHSQGYCGSNVKVAVIDSGIDSSHPDLKVAGGASM
VPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPCASLYAVKVLGADG
SGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVV
AAAGNEGTSGSSSTVGYPAKYPSVIAVGAVDSSNQRASFSSVGPELDVMA
PGVSIQSTLPGNKYGAYSGTSMASPHVAGAAALILSKHPNWTNTQVRSSL
ENTTTKLGDSFYYGKGLINVQAAAQ
3D structure
PDB1a2q Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D32 H64 N155 S221
Catalytic site (residue number reindexed from 1) D32 H64 N155 S221
Enzyme Commision number 3.4.21.62: subtilisin.
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 Q2 D41 L75 N77 I79 V81 Q2 D41 L75 N77 I79 V81
BS02 CA A A169 Y171 P172 V174 A169 Y171 P172 V174
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:1a2q, PDBe:1a2q, PDBj:1a2q
PDBsum1a2q
PubMed2684274
UniProtP00782|SUBT_BACAM Subtilisin BPN' (Gene Name=apr)

[Back to BioLiP]