Structure of PDB 2z30 Chain A

Receptor sequence

>2z30A (length=320) Species: 69014 (Thermococcus kodakarensis KOD1)

STQPAQTIPWGIERVKAPSVWSITDGSVSVIQVAVLDTGVDYDHPDLAAN
IAWCVSTLRGKVSTKLRDCADQNGHGTHVIGTIAALNNDIGVVGVAPGVQ
IYSVRVLDARGSGSYSDIAIGIEQAILGPDGVADKDGDGIIAGDPDDDAA
EVISMSLGGPADDSYLYDMIIQAYNAGIVIVAASGNEGAPSPSYPAAYPE
VIAVGAIDSNDNIASFSNRQPEVSAPGVDILSTYPDDSYETLMGTAMATP
HVSGVVALIQAAYYQKYGKILPVGTFDDISKNTVRGILHITADDLGPTGW
DADYGYGVVRAALAVQAALG

3D structure

• PDB: 2z30 Four new crystal structures of Tk-subtilisin in unautoprocessed, autoprocessed and mature forms: insight into structural changes during maturation
• Chain: A
• Resolution: 1.65 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D115 H153 N264 A324
• Catalytic site (residue number reindexed from 1): D37 H75 N186 A246
• 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	L205 G206 D208 V210 D226	L127 G128 D130 V132 D148
BS02	CA	A	D212 D214 D216 I218 D222 D225	D134 D136 D138 I140 D144 D147
BS03	CA	A	D214 D216 D222	D136 D138 D144
BS04	CA	A	V108 Q110 A227 E229	V30 Q32 A149 E151
BS05	CA	A	Q84 D124 L164 N166 I168 V170	Q6 D46 L86 N88 I90 V92
BS06	CA	A	D372 L373 P375 G377 D379	D294 L295 P297 G299 D301
BS07	CA	A	D119 D121 D314 D315	D41 D43 D236 D237

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:2z30, PDBe:2z30, PDBj:2z30
• PDBsum: 2z30
• PubMed: 17706669
• UniProt: P58502|TKSU_THEKO Tk-subtilisin (Gene Name=TK1675)