Research workbench
E. COLI methionine aminopeptidase in complex with nlep, 1: 2, di- metalated
Analyse E. COLI methionine aminopeptidase in complex with nlep, 1: 2, di- metalated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GU6
- Type
- protein
- Length
- 522 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
- NLP, MN, NA
- Pockets
- 5 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methionine aminopeptidase (EC 3.4.11.18) | protein | 261 | 29% helix, 28% strand | P0AE18 |
Ligands and binding sites
- NLP · (1-amino-pentyl)-phosphonic acid · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 339 | 0.61 | 0.78 | 40 | NLP |
| 2 | 128 | 0.58 | 0.84 | 26 | NLP |
| 3 | 158 | 0.48 | 0.77 | 28 | empty |
| 4 | 59 | 0.31 | 0.76 | 15 | empty |
| 5 | 64 | 0.28 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 508 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2GU6 · E. coli methionine aminopeptidase in complex with NleP, 1: 2, di-metalated · 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 0.99
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 2GU6 · PDBe 2GU6 · UniProt P0AE18
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.