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9L36

Cryo-electron microscopic structure of a novel amidohydrolase ADH3 triple mutation

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, D, E...
(A, B, C, D, E...)
Amidohydrolasepolymer40643373.88UniProt (A0A0S1B1B6)Stenotrophomonas sp. CW117
2AA, BA, DA, EA, I...
(G, H, A, B, C...)
ZINC IONnon-polymer65.416Chemie (ZN)
3CA, FA, K, N, Q...
(G, H, A, B, C...)
(2~{S})-2-[[(3~{R})-5-chloranyl-3-methyl-8-oxidanyl-1-oxidanylidene-3,4-dihydroisochromen-7-yl]carbonylamino]-3-phenyl-propanoic acidnon-polymer403.88Chemie (97U)
Sequence modifications
A, B, C, D, E, F, G, H: 22 - 427 (UniProt: A0A0S1B1B6)
PDBExternal DatabaseDetails
Arg 88Ser 88engineered mutation
Ala 184Thr 184conflict
Val 237Ala 237conflict
Ala 325Ile 325engineered mutation
Asn 344Asp 344engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains8
Total formula weight346990.2
Non-Polymers*Number of molecules24
Total formula weight4277.0
All*Total formula weight351267.3
*Water molecules are not included.

253389

PDB entries from 2026-05-13

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