Structure of PDB 1fjt Chain A

Receptor sequence
>1fjtA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB1fjt Experimental and computational mapping of the binding surface of a crystalline protein.
ChainA
Resolution2.2 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 ZN A H142 H146 E166 H142 H146 E166
BS02 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS03 CA A E177 N183 D185 E190 E177 N183 D185 E190
BS04 CA A D57 D59 Q61 D57 D59 Q61
BS05 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS06 VAL A E143 R203 E143 R203
BS07 LYS A N111 N112 F130 H231 N111 N112 F130 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:1fjt, PDBe:1fjt, PDBj:1fjt
PDBsum1fjt
PubMed11287678
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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