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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, D
(A, B, C, D)
GLYCOGEN PHOSPHORYLASEpolymer79690662.94UniProt (Q8KQ56)
Pfam (PF00343)
CORYNEBACTERIUM CALLUNAESTARCH PHOSPHORYLASE
2E, HA, P, Y
(A, D, B, C)
PYRIDOXAL-5'-PHOSPHATEnon-polymer247.14Chemie (PLP)
3AA, BA, F, IA, Q...
(C, A, D, B)
PHOSPHATE IONnon-polymer95.09Chemie (PO4)
4CA, DA, EA, FA, G...
(C, A, D, B)
FORMIC ACIDnon-polymer46.019Chemie (FMT)
5GA, W, X
(C, B)
1,2-ETHANEDIOLnon-polymer62.13Chemie (EDO)
6NA, OA, PA, QA
(A, B, C, D)
waterwater18.01154Chemie (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 2025-06-18

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