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2IUO

Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechanism of Cyanase

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, D, E...CYANATE HYDRATASEpolymer15617037.810UniProt (P00816)
Pfam (PF21291)
Pfam (PF02560)
In PDB
ESCHERICHIA COLICYANASE LYASE, CYANASE, CYANATE HYDROLASE
2E, F, A, G, B...BROMIDE IONnon-polymer79.910Chemie (BR)
3E, F, A, G, B...CHLORIDE IONnon-polymer35.510Chemie (CL)
4D, J, E, F, A...SULFATE IONnon-polymer96.123Chemie (SO4)
5BAZIDE IONnon-polymer42.01Chemie (AZI)
6waterwater18.02052Chemie (HOH)
Sequence modifications
A, B, C, D, E, F, G, H, I, J: 1 - 156 (UniProt: P00816)
PDBExternal DatabaseDetails
Gly 122Ser 122engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains10
Total formula weight170377.7
Non-Polymers*Number of molecules44
Total formula weight3405.0
All*Total formula weight173782.7
*Water molecules are not included.

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PDB entries from 2024-07-17

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