Research workbench
HsMetAP in complex with methionine
Analyse HsMetAP in complex with methionine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U6J
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.56
- Source
- Homo sapiens
- Molecule
- Methionine aminopeptidase 1
- EC
- 3.4.11.18
- UniProt
- P53582
- Ligands
- MET, CO, K
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · resolution 1.56 · 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
- MET · Methionine · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · chains A
- K · Potassium ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.61 | 0.78 | 42 | MET |
Compared structures
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 4U6J · PDBe 4U6J · UniProt P53582
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