Structure of PDB 2zrq Chain A

Receptor sequence

>2zrqA (length=318) Species: 69014 (Thermococcus kodakarensis KOD1)

QPAQTIPWGIERVKAPSVWSITDGSVSVIQVAVLDTGVDYDHPDLAANIA
WCVSTLRGKVSTKLRDCADQNGHGTHVIGTIAALNNDIGVVGVAPGVQIY
SVRVLDARGSGSYSDIAIGIEQAILGPDGVADKDGDGIIAGDPDDDAAEV
ISMSLGGPADDSYLYDMIIQAYNAGIVIVAASGNEGAPSPSYPAAYPEVI
AVGAIDSNDNIASFSNRQPEVSAPGVDILSTYPDDSYETLMGTAMATPHV
SGVVALIQAAYYQKYGKILPVGTFDDISKNTVRGILHITADDLGPTGWDA
DYGYGVVRAALAVQAALG

3D structure

• PDB: 2zrq Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding
• Chain: A
• Resolution: 2.16 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D115 H153 N264 A324
• Catalytic site (residue number reindexed from 1): D35 H73 N184 A244
• 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	Q4 D44 L84 N86 I88 V90
BS02	CA	A	V108 Q110 A227 E229	V28 Q30 A147 E149
BS03	CA	A	D119 D121 D314 D315	D39 D41 D234 D235
BS04	CA	A	L205 D208 V210 D226	L125 D128 V130 D146
BS05	CA	A	D212 D214 D216 I218 D222 D225	D132 D134 D136 I138 D142 D145
BS06	CA	A	D214 D216 D222 D224	D134 D136 D142 D144
BS07	CA	A	D372 L373 P375 G377 D379	D292 L293 P295 G297 D299

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:2zrq, PDBe:2zrq, PDBj:2zrq
• PDBsum: 2zrq
• PubMed: 18951896
• UniProt: P58502|TKSU_THEKO Tk-subtilisin (Gene Name=TK1675)