Structure of PDB 3a3n Chain A

Receptor sequence

>3a3nA (length=319) Species: 311400 (Thermococcus kodakarensis)

TQPAQTIPWGIERVKAPSVWSITDGSVSVIQVAVLDTGVDYDHPDLAANI
AWCVSTLRGKVSTKLRDCADQNGHGTHVIGTIAALNNDIGVVGVAPGVQI
YSVRVLDARGSGSYSDIAIGIEQAILGPDGVADKDGDGIIAGDPDDDAAE
VISMSLGGPADDSYLYDMIIQAYNAGIVIVAASGNEGAPSPSYPAAYPEV
IAVGAIDSNDNIASFSNRQPEVSAPGVDILSTYPDDSYETLMGTAMATPH
VSGVVALIQAAYYQKYGKILPVGTFDDISKNTVRGILHITADDLGPTGWD
ADYGYGVVRAALAVQAALG

3D structure

• PDB: 3a3n Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D115 H153 N264 A324
• Catalytic site (residue number reindexed from 1): D36 H74 N185 A245
• 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	Q84 D124 L164 N166 I168 V170	Q5 D45 L85 N87 I89 V91
BS02	CA	A	D119 D121 D314 D315	D40 D42 D235 D236
BS03	CA	A	L205 D208 V210 D226	L126 D129 V131 D147
BS04	CA	A	D212 D214 D216 I218 D222 D225	D133 D135 D137 I139 D143 D146
BS05	CA	A	D214 D216 D222	D135 D137 D143
BS06	CA	A	V108 Q110 A227 E229	V29 Q31 A148 E150
BS07	CA	A	D372 L373 G374 P375 G377 D379	D293 L294 G295 P296 G298 D300

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:3a3n, PDBe:3a3n, PDBj:3a3n
• PDBsum: 3a3n
• PubMed: 19766655
• UniProt: P58502|TKSU_THEKO Tk-subtilisin (Gene Name=TK1675)