Structure of PDB 3t8g Chain A

Receptor sequence
>3t8gA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB3t8g Water makes the difference: rearrangement of water solvation layer triggers non-additivity of functional group contributions in protein-ligand binding.
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H142 E143 H146 Y157 E166 D226 H231
Catalytic site (residue number reindexed from 1) H142 E143 H146 Y157 E166 D226 H231
Enzyme Commision number 3.4.24.27: thermolysin.
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 UBT A N112 A113 E143 H146 Y157 E166 L202 R203 H231 N112 A113 E143 H146 Y157 E166 L202 R203 H231 BindingDB: Ki=99999999999999nM
BS02 ZN A H142 H146 E166 H142 H146 E166
BS03 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS04 CA A E177 N183 D185 E190 E177 N183 D185 E190
BS05 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS06 CA A D57 D59 Q61 D57 D59 Q61
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3t8g, PDBe:3t8g, PDBj:3t8g
PDBsum3t8g
PubMed22733601
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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