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MolNFT v1 · #28948 · protein

Crystal structure of GLY19 deletion mutant of human acidic fibroblast growth factor

1YTO · Heparin-binding growth factor 1: “Crystal structure of GLY19 deletion mutant of human acidic fibroblast growth factor”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.60). MolNFT v1 #28948 on GenesisL1: 3D…

PDB
1YTO
Type
protein
Length
559 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heparin-binding growth factor 1
UniProt
P05230
Ligands
SO4
Pockets
4 · best druggability 0.60

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeparin-binding growth factor 1protein1399% helix, 37% strandP05230
B, CHeparin-binding growth factor 1protein1416% helix, 36% strandP05230
DHeparin-binding growth factor 1protein1387% helix, 40% strandP05230

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, C, D, B
  • FMT · Formic acid · additive · 3 copies · chains A, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14540.600.7550empty
21280.430.7620empty
31170.390.7520empty
4520.250.7316empty

Interfaces

3 interfaces between chains.

  • A–C · 439 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 424 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 106 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1YTO · Crystal Structure of Gly19 deletion Mutant of Human Acidic Fibroblast Growth Factor · the same entry in another collection · chain D against D, TM-score 1.00
  • P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain D against A, TM-score 0.97

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