Structure of PDB 2z2z Chain A

Receptor sequence

>2z2zA (length=389) Species: 69014 (Thermococcus kodakarensis KOD1)

NTIRVIVSVDKAKFNPHEVLGIGGHIVYQFKLIPAVVVDVPANAVGKLKK
MPGVEKVEFDHQAVLLGKPSWQPAQTIPWGIERVKAPSVWSITDGSVSVI
QVAVLDTGVDYDHPDLAANIAWCVSTLRGKVSTKLRDCADQNGHGTHVIG
TIAALNNDIGVVGVAPGVQIYSVRVLDARGSGSYSDIAIGIEQAILGPDG
VADKDGDGIIAGDPDDDAAEVISMSLGGPADDSYLYDMIIQAYNAGIVIV
AASGNEGAPSPSYPAAYPEVIAVGAIDSNDNIASFSNRQPEVSAPGVDIL
STYPDDSYETLMGTAMATPHVSGVVALIQAAYYQKYGKILPVGTFDDISK
NTVRGILHITADDLGPTGWDADYGYGVVRAALAVQAALG

3D structure

• PDB: 2z2z Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation
• Chain: A
• Resolution: 1.87 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D115 H153 N264 A324
• Catalytic site (residue number reindexed from 1): D106 H144 N255 A315
• 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	V108 Q110 A227 E229	V99 Q101 A218 E220
BS02	CA	A	D119 D121 D314 D315	D110 D112 D305 D306
BS03	CA	A	L205 D208 V210 D226	L196 D199 V201 D217
BS04	CA	A	D212 D214 D216 I218 D222 D225	D203 D205 D207 I209 D213 D216
BS05	CA	A	D214 D216 D222 D224	D205 D207 D213 D215
BS06	CA	A	D372 L373 P375 G377 D379	D363 L364 P366 G368 D370
BS07	CA	A	Q84 D124 L164 N166 I168 V170	Q75 D115 L155 N157 I159 V161

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:2z2z, PDBe:2z2z, PDBj:2z2z
• PDBsum: 2z2z
• PubMed: 17706669
• UniProt: P58502|TKSU_THEKO Tk-subtilisin (Gene Name=TK1675)