MolNFT v1 · #16461 · protein
Crystal structure of a multiple mutant (L44F, L73V, V109L, L111I, C117V) of human acidic fibroblast growth factor
1NZK: “Crystal structure of a multiple mutant (L44F, L73V, V109L, L111I, C117V) of human acidic fibroblast growth…”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.38). MolNFT v1 #16461 on GenesisL1: 3D structure…
- PDB
- 1NZK
- Type
- protein
- Length
- 564 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic fibroblast growth factor
- UniProt
- P05230
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Acidic fibroblast growth factor | protein | 141 | 6% helix, 40% strand | P05230 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- FMT · Formic acid · additive · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.38 | 0.76 | 18 | empty |
| 2 | 89 | 0.35 | 0.75 | 21 | empty |
Interfaces
2 interfaces between chains.
- C–D · 453 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 449 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1NZK · Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic… · 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 B against A, TM-score 0.96
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 P05230
- Elsewhere: RCSB PDB 1NZK · PDBe 1NZK · UniProt P05230
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