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5EHT

Indirect contributions of mutations underlie optimization of new enzyme function

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A
(A)
N-acyl homoserine lactonasepolymer25328468.31UniProt (A3FJ64)
Pfam (PF00753)
Bacillus thuringiensisAHL-lactonase,Homoserine lactone lactonase
2B, C
(A)
ZINC IONnon-polymer65.42Chemie (ZN)
3D, E, F, G, H...
(A)
GLYCEROLnon-polymer92.16Chemie (GOL)
4J
(A)
waterwater18.0247Chemie (HOH)
Sequence modifications
A: 2 - 250 (UniProt: A3FJ64)
PDBExternal DatabaseDetails
Gly -2-expression tag
His -1-expression tag
Met 0-expression tag
Ala 1-expression tag
Val 9Ile 9engineered mutation
Phe 20Ser 20engineered mutation
Val 33Leu 33engineered mutation
Cso 64Phe 64engineered mutation
Gly 69Val 69engineered mutation
Thr 139Lys 139engineered mutation
Met 230Ile 230engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains1
Total formula weight28468.3
Non-Polymers*Number of molecules8
Total formula weight683.4
All*Total formula weight29151.7
*Water molecules are not included.

246905

PDB entries from 2025-12-31

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