Structure of PDB 3dnz Chain A

Receptor sequence
>3dnzA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB3dnz Radiation damage in protein structural characterization by Synchrotron Radiation: State of the art and Nanotechnology-based perspective
ChainA
Resolution1.2 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 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS02 CA A E177 N183 P184 D185 E190 E177 N183 P184 D185 E190
BS03 CA A D57 D59 Q61 D57 D59 Q61
BS04 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS05 ZN A H142 H146 E166 H142 H146 E166
BS06 VAL A N112 A113 E143 R203 N112 A113 E143 R203
BS07 LYS A N112 L202 H231 N112 L202 H231
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:3dnz, PDBe:3dnz, PDBj:3dnz
PDBsum3dnz
PubMed
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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