Research workbench
Hsmetap in complex with (AMINO(PHENYL)METHYL)PHOSPHONIC acid
Analyse Hsmetap in complex with (AMINO(PHENYL)METHYL)PHOSPHONIC acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4U6E
- 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
- Q02, CO
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 1 (EC 3.4.11.18) | protein | 304 | 26% helix, 22% strand | P53582 |
Ligands and binding sites
- Q02 · [(R)-amino(phenyl)methyl]phosphonic acid · ligand · chains A
- CO · Cobalt (II) ion · metal · 2 copies · 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 | 266 | 0.57 | 0.77 | 40 | Q02 |
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 4U6E · PDBe 4U6E · UniProt P53582
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