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2YCE

Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.

Replaces:  1W8R
Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, D, E...
(A, B, C, D, E...)
FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1polymer26328741.110UniProt (P58315)
Pfam (PF01791)
THERMOPROTEUS TENAXFRUCTOSE-BIPHOSPHATE ALDOLASE CLASS I, FBP ALDOLASE
2K, L, M, N, O...
(A, B, C, D, E...)
D-MANNITOL-1,6-DIPHOSPHATEnon-polymer342.110Chemie (M2P)
PubChem (23644175)
PubChem (44448097)
PubChem (449501)
PubChem (4369446)
PubChem (5288174)
3AA, BA, CA, DA, U...
(G, H, I, J, A...)
waterwater18.01518Chemie (HOH)
Sequence modifications
A, B, C, D, E, F, G, H, I, J: 1 - 263 (UniProt: P58315)
PDBExternal DatabaseDetails
Phe 146Tyr 146engineered mutation
Ser 173Ala 173engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains10
Total formula weight287410.6
Non-Polymers*Number of molecules10
Total formula weight3421.3
All*Total formula weight290832.0
*Water molecules are not included.

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PDB entries from 2026-05-20

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