Research workbench
Crystal structure of methionine amino peptidase in complex with N-cyclopentyl-N-(thiazol-2-YL)OXALAMIDE
Analyse Crystal structure of methionine amino peptidase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EVO
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine aminopeptidase
- EC
- 3.4.11.18
- UniProt
- P0AE18
- Ligands
- CT0, CO
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methionine aminopeptidase (EC 3.4.11.18) | protein | 260 | 28% helix, 28% strand | P0AE18 |
Ligands and binding sites
- CT0 · N1-cyclopentyl-N2-(thiazol-2-yl)oxalamide · ligand · 2 copies · chains A, B
- CO · Cobalt (II) ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.59 | 0.77 | 44 | CO, CT0 |
| 2 | 127 | 0.57 | 0.84 | 27 | CO, CT0 |
| 3 | 290 | 0.53 | 0.75 | 38 | empty |
| 4 | 58 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 442 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2EVO · crystal structure of methionine amino peptidase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AE18 · AlphaFold monomer V2.0 prediction for methionine aminopeptidase (P0AE18) · 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 P0AE18
- Elsewhere: RCSB PDB 2EVO · PDBe 2EVO · UniProt P0AE18
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