Structure of PDB 6d5t Chain A

Receptor sequence
>6d5tA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB6d5t The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.
ChainA
Resolution2.00004 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 VAL A N112 E143 R203 N112 E143 R203
BS02 LYS A N112 H231 N112 H231
BS03 ZN A H142 H146 E166 H142 H146 E166
BS04 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS05 CA A D57 D59 Q61 D57 D59 Q61
BS06 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS07 CA A E177 N183 D185 E190 E177 N183 D185 E190
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:6d5t, PDBe:6d5t, PDBj:6d5t
PDBsum6d5t
PubMed30198901
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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