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3G8D

Crystal structure of the biotin carboxylase subunit, E296A mutant, of acetyl-COA carboxylase from Escherichia coli

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B
(A, B)
Biotin carboxylasepolymer44448772.02UniProt (P24182)
Pfam (PF00289)
Pfam (PF02786)
Pfam (PF02785)
Escherichia coliAcetyl-CoA carboxylase subunit A, ACC
2C, F
(A, B)
SULFATE IONnon-polymer96.12Chemie (SO4)
3D
(B)
ADENOSINE-5'-DIPHOSPHATEnon-polymer427.21Chemie (ADP)
4E
(B)
MAGNESIUM IONnon-polymer24.31Chemie (MG)
5G, H
(A, B)
waterwater18.0478Chemie (HOH)
Sequence modifications
A, B: 1 - 444 (UniProt: P24182)
PDBExternal DatabaseDetails
Ala 296Glu 296engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains2
Total formula weight97544.0
Non-Polymers*Number of molecules4
Total formula weight643.6
All*Total formula weight98187.6
*Water molecules are not included.

250059

PDB entries from 2026-03-04

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