MolNFT v1 · #172391 · protein
Crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor GSK2218325A (compound 32)
7A14 · Methionine aminopeptidase 2: “Crystal structure of human methionine aminopeptidase-2 in complex with an inhibitor GSK2218325A (compound 32)”. X-ray diffraction, 3 ligands (QVB, MN, PO4), 3 pockets (best druggability 0.68). MolNFT v1…
- PDB
- 7A14
- Type
- protein
- Length
- 366 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
- QVB, MN, PO4
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2 (EC 3.4.11.18) | protein | 366 | 33% helix, 25% strand | P50579 |
Ligands and binding sites
- QVB · 5-chloranyl-6-fluoranyl-3-(2-propan-2-yloxyphenyl)-1~{H}-indole-2-carboxamide · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.68 | 0.84 | 41 | QVB |
| 2 | 56 | 0.46 | 0.84 | 16 | empty |
| 3 | 64 | 0.28 | 0.73 | 13 | PO4 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7A14 · Crystal structure of human methionine aminopeptidase-2 in complex with an 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 7A14 · PDBe 7A14 · UniProt P50579
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