Structure of PDB 4h57 Chain A

Receptor sequence
>4h57A (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB4h57 Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin.
ChainA
Resolution1.56 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 D185 E190 E177 N183 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 0PJ A N112 A113 F114 F130 E143 H146 Y157 E166 L202 R203 H231 N112 A113 F114 F130 E143 H146 Y157 E166 L202 R203 H231 BindingDB: Ki=99999999999999nM
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:4h57, PDBe:4h57, PDBj:4h57
PDBsum4h57
PubMed23283700
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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