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Anisotropically refined structure of ftcd

Analyse Anisotropically refined structure of ftcd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DFormimidoyltransferase-cyclodeaminase (EC 2.1.2.5, 4.3.1.4)protein54051% helix, 14% strandO88618

Pockets

17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13130.660.8131empty
22820.640.8128empty
33040.640.8032empty
43160.630.8032empty
54770.600.7541empty

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

  • 2PFD · Anisotropically refined structure of FTCD · the same entry in another collection · chain D against D, TM-score 1.00
  • O88618 · AlphaFold monomer V2.0 prediction for formimidoyltransferase- cyclodeaminase (O88618) · a predicted model of the same protein · chain B against A, TM-score 0.87

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