Current Protein Identity:Q9NWU1
New Search
Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 2C9H Structure of mitochondrial beta-ketoacyl synthase Deposited 2005-12-12 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
39–459(421 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | NI NICKEL (II) ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 5.5;0.1 M BIS-TRIS PH=5.5, 25% PEG3350, 0.20 M NH4AC, pH 5.50
|
Resolution 1.80 Å R-free 0.240 |
| 2IWY Human mitochondrial beta-ketoacyl ACP synthase Deposited 2006-07-05 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
38–459(422 aa)
Fragment:RESIDUES 38-459
Chain B
38–459(422 aa)
Fragment:RESIDUES 38-459
|
Not recorded | NH4 AMMONIUM ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.8;24% PEG-3350, 0.2 M NH4CL, pH 7.80
|
Resolution 2.06 Å R-free 0.205 |
| 2IWZ Human mitochondrial beta-ketoacyl ACP synthase complexed with hexanoic acid Deposited 2006-07-05 | Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count |
Chain A
38–459(422 aa)
Fragment:RESIDUES 38-459
Chain B
38–459(422 aa)
Fragment:RESIDUES 38-459
|
Not recorded | 6NA HEXANOIC ACID × 2 NH4 AMMONIUM ION × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.8;24% PEG3350, 0.2M NH4CL, pH 7.80
|
Resolution 1.65 Å R-free 0.188 |
| 9N50 Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and Crosslinker-crypto Human Mitochondrial Acyl Carrier Protein, C8aBr-mACP Deposited 2025-02-03 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain A
38–459(422 aa)
Fragment:residues 38-459
Chain B
38–459(422 aa)
Fragment:residues 38-459
|
Not recorded | A1BMZ N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethyl)-beta-alaninamide × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;293 K;0.5 M ammonium sulfate, 1 M lithium sulfate, and 0.1 M sodium citrate pH 5.6
|
Resolution 2.50 Å |
| 9N51 Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and Crosslinker-crypto Human Mitochondrial Acyl Carrier Protein, C8Cl-mACP Deposited 2025-02-03 | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain A
38–459(422 aa)
Fragment:residues 38-459
Chain B
38–459(422 aa)
Fragment:residues 38-459
|
Not recorded | A1BMZ N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethyl)-beta-alaninamide × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;293 K;0.5 M ammonium sulfate, 1 M lithium sulfate, and 0.1 M sodium citrate pH 5.6
|
Resolution 2.31 Å R-free 0.273 |
| 9N51 Crosslinked Crystal Structure of Human Mitochondrial Ketosynthase, OXSM, and Crosslinker-crypto Human Mitochondrial Acyl Carrier Protein, C8Cl-mACP Deposited 2025-02-03 | Assembly 2 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count |
Chain D
38–459(422 aa)
Fragment:residues 38-459
Chain E
38–459(422 aa)
Fragment:residues 38-459
|
Not recorded | A1BMZ N~3~-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-octanamidoethyl)-beta-alaninamide × 1 | X-RAY DIFFRACTION |
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;293 K;0.5 M ammonium sulfate, 1 M lithium sulfate, and 0.1 M sodium citrate pH 5.6
|
Resolution 2.31 Å R-free 0.273 |