Research workbench
Human fatty acid synthase PSI/KR tri-domain with NADPH and compound 22
Analyse Human fatty acid synthase PSI/KR tri-domain with NADPH and compound 22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NNA
- Type
- protein
- Length
- 1,216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid SYNTHASE,FATTY acid synthase
- EC
- 2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.59, 1.3.1.39, 3.1.2.14
- UniProt
- P49327
- Ligands
- NDP, KUA
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid SYNTHASE,FATTY acid synthase (EC 2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.59, 1.3.1.39, 3.1.2.14) | protein | 608 | 40% helix, 23% strand | P49327 |
| B | Fatty acid SYNTHASE,FATTY acid synthase (EC 2.3.1.85, 2.3.1.38, 2.3.1.39, 2.3.1.41, 1.1.1.100, 4.2.1.59, 1.3.1.39, 3.1.2.14) | protein | 608 | 39% helix, 23% strand | P49327 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- KUA · {4-[4-(1,3-benzoxazol-2-yl)benzene-1-carbonyl]piperazin-1-yl}(1-hydroxycyclopropyl) methanone · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.83 | 0.86 | 84 | NDP, KUA, EDO |
| 2 | 882 | 0.82 | 0.84 | 93 | NDP, KUA, EDO |
| 3 | 581 | 0.66 | 0.77 | 38 | EDO |
| 4 | 464 | 0.61 | 0.76 | 49 | empty |
| 5 | 125 | 0.55 | 0.82 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 496 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6NNA · Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and Compound 22 · the same entry in another collection · chain A against A, TM-score 1.00
- P49327 · AlphaFold monomer V2.0 prediction for fatty acid synthase (P49327) · a predicted model of the same protein · chain B against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P49327
- Elsewhere: RCSB PDB 6NNA · PDBe 6NNA · UniProt P49327
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