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MolNFT v1 · #46068 · protein

Human fibroblast growth factor-1 (140 amino acid form) with CYS117VAL/PRO134CYS mutations

2NTD · Acidic fibroblast growth factor 1: “Human fibroblast growth factor-1 (140 amino acid form) with CYS117VAL/PRO134CYS mutations”. X-ray diffraction, 7 pockets (best druggability 0.76). MolNFT v1 #46068 on GenesisL1: 3D structure…

PDB
2NTD
Type
protein
Length
569 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acidic fibroblast growth factor 1
UniProt
P05230
Pockets
7 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, DAcidic fibroblast growth factor 1protein1424% helix, 39% strandP05230
BAcidic fibroblast growth factor 1protein1436% helix, 37% strandP05230

Ligands and binding sites

  • FMT · Formic acid · additive · 11 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17210.760.8178empty
21680.610.8334empty
31540.590.8329empty
41390.380.7326empty
5740.330.7413FMT

Interfaces

5 interfaces between chains.

  • A–B · 709 Ų buried · 20 hydrogen bonds · protein-protein
  • C–D · 704 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 642 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 588 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 201 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2NTD · Human fibroblast growth factor-1 (140 amino acid form) with Cys117Val/Pro134Cys mutations · 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 0.95

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