Structure of PDB 5ffn Chain A

Receptor sequence
>5ffnA (length=311) Species: 1409 (Bacillus sp. (in: firmicutes)) [Search protein sequence]
AVPSTQTPWGIKSIYNDQSITKTTGGSGIKVAVLDTGVYTSHLDLAGSAE
QCKDFTQSNPLVDGSCTDRQGHGTHVAGTVLAHGGSNGQGVYGVAPQAKL
WAYKVLGDNGSGYSDDIAAAIRHVADEASRTGSKVVINMSLGSSAKDSLI
ASAVDYAYGKGVLIVAAAGNSGSGSNTIGFPGGLVNAVAVAALENVQQNG
TYRVADFSSRGNPATAGDYIIQERDIEVSAPGASVESTWYTGGYNTISGT
SMATPHVAGLAAKIWSANTSLSHSQLRTELQNRAKVYDIKGGIGAGTGDD
YASGFGYPRVK
3D structure
PDB5ffn Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family
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) D35 H72 N170 S251
Catalytic site (residue number reindexed from 1) D35 H72 N170 S251
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.
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 T215 D218 I220 Q222 D225 T215 D218 I220 Q222 D225
BS02 CA A D288 I289 G296 G298 D300 D288 I289 G296 G298 D300
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5ffn, PDBe:5ffn, PDBj:5ffn
PDBsum5ffn
PubMed
UniProtA0A182DWC8

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