MolNFT v1 · #37707 · protein
H-METAP2 complexed with A193400
2GA2 · Methionine aminopeptidase 2: “H-METAP2 complexed with A193400”. X-ray diffraction, 2 ligands (A19, MN), 2 pockets (best druggability 0.68). MolNFT v1 #37707 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GA2
- Type
- protein
- Length
- 369 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
- A19, MN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2 (EC 3.4.11.18) | protein | 369 | 31% helix, 25% strand | P50579 |
Ligands and binding sites
- A19 · 5-bromo-2-{[(4-chlorophenyl)sulfonyl]amino}benzoic acid · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.68 | 0.83 | 39 | A19 |
| 2 | 77 | 0.34 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P50579
- Elsewhere: RCSB PDB 2GA2 · PDBe 2GA2 · UniProt P50579
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