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Crystal Structure of apo human FABP1 - orthorhombic form

Analyse Crystal Structure of apo human FABP1 - orthorhombic form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7FYA
Type
protein
Length
259 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.88
Source
Homo sapiens
Molecule
Fatty acid-binding protein, liver
UniProt
P07148
Pockets
5 · best druggability 0.84

Structure

x-ray diffraction · resolution 1.88 · 2 distinct chains · 12% helix, 59% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFatty acid-binding protein, liverprotein12912% helix, 59% strandP07148
BFatty acid-binding protein, liverprotein13012% helix, 58% strandP07148

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12410.840.9637empty
22660.840.9537empty
3560.540.8927empty
4690.340.7615empty
5610.330.7722empty

Interfaces

1 interface between chains.

  • A–B · 667 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • P07148 · AlphaFold monomer V2.0 prediction for fatty acid-binding protein, liver (P07148) · a predicted model of the same protein · chain A against A, TM-score 0.94

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