MolNFT v1 · #47986 · protein
Anisotropically refined structure of ftcd
2PFD · Formimidoyltransferase-cyclodeaminase: “Anisotropically refined structure of ftcd”. X-ray diffraction, 17 pockets (best druggability 0.66). MolNFT v1 #47986 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PFD
- Type
- protein
- Length
- 2,160 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formimidoyltransferase-cyclodeaminase
- EC
- 2.1.2.5, 4.3.1.4
- UniProt
- O88618
- Pockets
- 17 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Formimidoyltransferase-cyclodeaminase (EC 2.1.2.5, 4.3.1.4) | protein | 540 | 51% helix, 14% strand | O88618 |
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.66 | 0.81 | 31 | empty |
| 2 | 282 | 0.64 | 0.81 | 28 | empty |
| 3 | 304 | 0.64 | 0.80 | 32 | empty |
| 4 | 316 | 0.63 | 0.80 | 32 | empty |
| 5 | 477 | 0.60 | 0.75 | 41 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2411 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 2387 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 266 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
Compared structures
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 O88618
- Elsewhere: RCSB PDB 2PFD · PDBe 2PFD · UniProt O88618
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