Research workbench
Human methionine aminopeptidase in complex with FZ1: pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1
Analyse Human methionine aminopeptidase in complex with FZ1: pyridinylquinazolines… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IU6
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase 1
- EC
- 3.4.11.18
- UniProt
- P53582
- Ligands
- FZ1, CO, K, SO4
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 1 (EC 3.4.11.18) | protein | 304 | 27% helix, 22% strand | P53582 |
Ligands and binding sites
- FZ1 · 4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline · ligand · chains A
- CO · Cobalt (II) ion · metal · 3 copies · chains A
- K · Potassium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.65 | 0.95 | 20 | empty |
| 2 | 307 | 0.59 | 0.78 | 41 | CO, FZ1 |
Compared structures
- 4IU6 · Human Methionine Aminopeptidase in complex with FZ1: Pyridinylquinazolines Selectively… · the same entry in another collection · chain A against A, TM-score 1.00
- P53582 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 1 (P53582) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P53582
- Elsewhere: RCSB PDB 4IU6 · PDBe 4IU6 · UniProt P53582
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