Structure of PDB 5tmn Chain E

Receptor sequence
>5tmnE (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB5tmn Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.
ChainE
Resolution1.6 Å
3D
structure
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Enzymatic activity
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 0PJ E N112 A113 F114 F130 E143 H146 Y157 L202 R203 H231 N112 A113 F114 F130 E143 H146 Y157 L202 R203 H231 MOAD: Ki=9.1nM
PDBbind-CN: -logKd/Ki=8.04,Ki=9.1nM
BindingDB: Ki=99999999999999nM
BS02 CA E D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS03 CA E E177 N183 D185 E190 E177 N183 D185 E190
BS04 CA E D57 D59 Q61 D57 D59 Q61
BS05 CA E Y193 T194 I197 D200 Y193 T194 I197 D200
BS06 ZN E H142 H146 E166 H142 H146 E166
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:5tmn, PDBe:5tmn, PDBj:5tmn
PDBsum5tmn
PubMed3442675
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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