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2C4M

Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.

Entity
Entity IDChain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
1A, B, C, DGLYCOGEN PHOSPHORYLASEpolymer79690662.94UniProt (Q8KQ56)
Pfam (PF00343)
In PDB
CORYNEBACTERIUM CALLUNAESTARCH PHOSPHORYLASE
2A, D, B, CPYRIDOXAL-5'-PHOSPHATEnon-polymer247.14Chemie (PLP)
3C, A, D, BPHOSPHATE IONnon-polymer95.09Chemie (PO4)
4C, A, D, BFORMIC ACIDnon-polymer46.019Chemie (FMT)
5C, B1,2-ETHANEDIOLnon-polymer62.13Chemie (EDO)
6waterwater18.01154Chemie (HOH)
Sequence modifications
A, B, C, D: 0 - 795 (UniProt: Q8KQ56)
PDBExternal DatabaseDetails
Ala 224Ser 225engineered mutation
Sequence viewer
Contents of the asymmetric unit
PolymersNumber of chains4
Total formula weight362651.7
Non-Polymers*Number of molecules35
Total formula weight2904.0
All*Total formula weight365555.7
*Water molecules are not included.

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PDB entries from 2024-07-31

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