Research workbench
Human guanylate binding protein-1 in complex with the GTP analogue, gmppnp.
Analyse Human guanylate binding protein-1 in complex with the GTP analogue, gmppnp. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F5N
- Type
- protein
- Length
- 570 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced guanylate-binding protein 1
- UniProt
- P32455
- Ligands
- GNP, MG
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-induced guanylate-binding protein 1 | protein | 570 | 63% helix, 11% strand | P32455 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.73 | 0.86 | 48 | MG, GNP |
| 2 | 625 | 0.72 | 0.80 | 68 | empty |
| 3 | 134 | 0.61 | 0.85 | 26 | empty |
| 4 | 165 | 0.45 | 0.75 | 29 | empty |
| 5 | 82 | 0.45 | 0.81 | 20 | empty |
Compared structures
- 1F5N · Human guanylate binding protein-1 in complex with the GTP analogue, gmppnp. · the same entry in another collection · chain A against A, TM-score 1.00
- P32455 · AlphaFold monomer V2.0 prediction for guanylate-binding protein 1 (P32455) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P32455
- Elsewhere: RCSB PDB 1F5N · PDBe 1F5N · UniProt P32455
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