Research workbench
Human methionine aminopeptidase complex with 4-aryl-1,2,3-triazole inhibitor
Analyse Human methionine aminopeptidase complex with 4-aryl-1,2,3-triazole inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ADU
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase 2
- EC
- 3.4.11.18
- UniProt
- P50579
- Ligands
- R20, CO
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2 (EC 3.4.11.18) | protein | 355 | 31% helix, 27% strand | P50579 |
Ligands and binding sites
- R20 · 4-(3-methylphenyl)-1H-1,2,3-triazole · 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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.66 | 0.85 | 36 | R20 |
| 2 | 58 | 0.49 | 0.85 | 17 | empty |
| 3 | 51 | 0.28 | 0.75 | 20 | empty |
| 4 | 50 | 0.24 | 0.72 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2ADU · Human Methionine Aminopeptidase Complex with 4-Aryl-1,2,3-triazole Inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- P50579 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase 2 (P50579) · 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 P50579
- Elsewhere: RCSB PDB 2ADU · PDBe 2ADU · UniProt P50579
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