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Enzymes
  Enzyme classes:
  EC 1: Oxidoreductases
  EC 2: Transferases
  EC 3: Hydrolases
  EC 4: Lyases
    EC 4.1
      EC 4.1.1
      EC 4.1.2
      EC 4.1.3
        EC 4.1.3.1
        EC 4.1.3.2
        EC 4.1.3.3
        EC 4.1.3.4
        EC 4.1.3.5
        EC 4.1.3.6
        EC 4.1.3.7
        EC 4.1.3.8
        EC 4.1.3.9
        EC 4.1.3.10
        EC 4.1.3.11
        EC 4.1.3.12
        EC 4.1.3.13
        EC 4.1.3.14
        EC 4.1.3.15
        EC 4.1.3.16
        EC 4.1.3.17
        EC 4.1.3.18
        EC 4.1.3.19
        EC 4.1.3.20
        EC 4.1.3.21
        EC 4.1.3.22
        EC 4.1.3.23
        EC 4.1.3.24
        EC 4.1.3.25
        EC 4.1.3.26
        EC 4.1.3.27
        EC 4.1.3.28
        EC 4.1.3.29
        EC 4.1.3.30
        EC 4.1.3.31
        EC 4.1.3.32
        EC 4.1.3.33
        EC 4.1.3.34
        EC 4.1.3.35
        EC 4.1.3.36
        EC 4.1.3.37
        EC 4.1.3.38
        EC 4.1.3.39
        EC 4.1.3.40
      EC 4.1.99
    EC 4.2
    EC 4.3
    EC 4.4
    EC 4.5
    EC 4.6
    EC 4.99
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 4.1.3.6 - citrate oxaloacetate- lyase (forming acetate from the pro - S carboxymethyl group of citrate) (citrate ( pro- 3 S ) - lyase)

3D structures of EC 4.1.3.6 - citrate (pro-3S)-lyase in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 5 PDB structures of EC 4.1.3.6 - citrate (pro-3S)-lyase:

1u5h: Structure of Citrate Lyase Beta Subunit from Mycobacterium Tuberculosis
1u5v: Structure of Cite Complexed with Triphosphate Group of Atp Form Mycobacterium Tuberculosis
1z6k: Citrate Lyase Beta Subunit Complexed with Oxaloacetate and Magnesium from M. Tuberculosis
2hj0: Crystal Structure of The Putative Alfa Subunit of Citrate Lyase in Complex with Citrate from Streptococcus Mutans, Northeast Structural Genomics Target Smr12 (casp Target).
3r4i: Crystal Structure of a Citrate Lyase (bxe_b2899) from Burkholderia Xenovorans Lb400 at 2.24 a Resolution